scholarly journals The TMCrys server for supporting crystallization of transmembrane proteins

2019 ◽  
Vol 35 (20) ◽  
pp. 4203-4204
Author(s):  
Julia K Varga ◽  
Gábor E Tusnády
Keyword(s):  
Membrane Proteins ◽  
Structure Determination ◽  
Web Server ◽  
Transmembrane Proteins ◽  
Prediction Method ◽  
Supplementary Information ◽  
Supplementary Data ◽  
Successful Completion ◽  
Determination Process

Abstract Motivation Due to their special properties, the structures of transmembrane proteins are extremely hard to determine. Several methods exist to predict the propensity of successful completion of the structure determination process. However, available predictors incorporate data of any kind of proteins, hence they can hardly differentiate between crystallizable and non-crystallizable membrane proteins. Results We implemented a web server to simplify running TMCrys prediction method that was developed specifically to separate crystallizable and non-crystallizable membrane proteins. Availability and implementation http://tmcrys.enzim.ttk.mta.hu Supplementary information Supplementary data are available at Bioinformatics online.

scholarly journals The TMCrys server for supporting crystallization of transmembrane proteins

2018 ◽  
Author(s):  
Julia K. Varga ◽  
Gábor E. Tusnády
Keyword(s):  
Membrane Proteins ◽  
Structure Determination ◽  
Web Server ◽  
Transmembrane Proteins ◽  
Prediction Method ◽  
Successful Completion ◽  
Link Type ◽  
Determination Process

AbstractMotivationDue to their special properties, the structures of transmembrane proteins are extremely hard to determine. Several methods exist to predict the propensity of successful completion of the structure determination process. However, available predictors incorporate data of any kind of proteins, hence they can hardly differentiate between crystallizable and non-crystallizable membrane proteins.ResultsWe implemented a web server to simplify running TMCrys prediction method that was developed specifically to separate crystallizable and non-crystallizable proteins.Availabilityhttp://tmcrys.enzim.ttk.mta.huContacttusnady.gabor@[email protected]

Inter-residue interactions in alpha-helical transmembrane proteins

2018 ◽  
Vol 35 (15) ◽  
pp. 2578-2584 ◽  
Author(s):  
Eduardo Mayol ◽  
Mercedes Campillo ◽  
Arnau Cordomí ◽  
Mireia Olivella
Keyword(s):  
Membrane Proteins ◽  
Present Report ◽  
Protein Structures ◽  
Transmembrane Proteins ◽  
Globular Proteins ◽  
Supplementary Information ◽  
Backbone Carbonyl ◽  
Composition Characteristic ◽  
Almost All ◽  
Residue Composition

Abstract Motivation The number of available membrane protein structures has markedly increased in the last years and, in parallel, the reliability of the methods to detect transmembrane (TM) segments. In the present report, we characterized inter-residue interactions in α-helical membrane proteins using a dataset of 3462 TM helices from 430 proteins. This is by far the largest analysis published to date. Results Our analysis of residue–residue interactions in TM segments of membrane proteins shows that almost all interactions involve aliphatic residues and Phe. There is lack of polar–polar, polar–charged and charged–charged interactions except for those between Thr or Ser sidechains and the backbone carbonyl of aliphatic and Phe residues. The results are discussed in the context of the preferences of amino acids to be in the protein core or exposed to the lipid bilayer and to occupy specific positions along the TM segment. Comparison to datasets of β-barrel membrane proteins and of α-helical globular proteins unveils the specific patterns of interactions and residue composition characteristic of α-helical membrane proteins that are the clue to understanding their structure. Availability and implementation Results data and datasets used are available at http://lmc.uab.cat/TMalphaDB/interactions.php. Supplementary information Supplementary data are available at Bioinformatics online.

scholarly journals COVID-19 Docking Server: a meta server for docking small molecules, peptides and antibodies against potential targets of COVID-19

2020 ◽  
Vol 36 (20) ◽  
pp. 5109-5111 ◽  
Author(s):  
Ren Kong ◽  
Guangbo Yang ◽  
Rui Xue ◽  
Ming Liu ◽  
Feng Wang ◽  
...  
Keyword(s):  
Life Cycle ◽  
Drug Discovery ◽  
Small Molecules ◽  
Web Server ◽  
Supplementary Information ◽  
Binding Modes ◽  
Supplementary Data ◽  
Virus Life Cycle ◽  
Ligand Interactions ◽  
New Type

Abstract Motivation The coronavirus disease 2019 (COVID-19) caused by a new type of coronavirus has been emerging from China and led to thousands of death globally since December 2019. Despite many groups have engaged in studying the newly emerged virus and searching for the treatment of COVID-19, the understanding of the COVID-19 target–ligand interactions represents a key challenge. Herein, we introduce COVID-19 Docking Server, a web server that predicts the binding modes between COVID-19 targets and the ligands including small molecules, peptides and antibodies. Results Structures of proteins involved in the virus life cycle were collected or constructed based on the homologs of coronavirus, and prepared ready for docking. The meta-platform provides a free and interactive tool for the prediction of COVID-19 target–ligand interactions and following drug discovery for COVID-19. Availability and implementation http://ncov.schanglab.org.cn. Supplementary information Supplementary data are available at Bioinformatics online.

scholarly journals DR-SIP: protocols for higher order structure modeling with distance restraints- and cyclic symmetry-imposed packing

2019 ◽  
Author(s):  
Justin Chan ◽  
Jinhao Zou ◽  
Christopher Llynard Ortiz ◽  
Chi-Hong Chang Chien ◽  
Rong-Long Pan ◽  
...  
Keyword(s):  
Structure Determination ◽  
Quaternary Structure ◽  
Transmembrane Proteins ◽  
Supplementary Information ◽  
Order Structure ◽  
Structure Modeling ◽  
Cyclic Symmetry ◽  
X Ray ◽  
Distance Restraints ◽  
Symmetric Complex

Abstract Motivation Quaternary structure determination for transmembrane/soluble proteins requires a reliable computational protocol that leverages observed distance restraints and/or cyclic symmetry (Cn symmetry) found in most homo-oligomeric transmembrane proteins. Results We survey 118 X-ray crystallographically solved structures of homo-oligomeric transmembrane proteins (HoTPs) and find that ∼97% are Cn symmetric. Given the prevalence of Cn symmetric HoTPs and the benefits of incorporating geometry restraints in aiding quaternary structure determination, we introduce two new filters, the distance-restraints (DR) and the Symmetry-Imposed Packing (SIP) filters. SIP relies on a new method that can rebuild the closest ideal Cn symmetric complex from docking poses containing a homo-dimer without prior knowledge of the number (n) of monomers. Using only the geometrical filter, SIP, near-native poses of 7 HoTPs in their monomeric states can be correctly identified in the top-10 for 71% of all cases, or 29% among 31 HoTP structures obtained through homology modeling, while ZDOCK alone returns 14 and 3%, respectively. When the n is given, the optional n-mer filter is applied with SIP and returns the near-native poses for 76% of the test set within the top-10, outperforming M-ZDOCK’s 55% and Sam’s 47%. While applying only SIP to three HoTPs that comes with distance restraints, we found the near-native poses were ranked 1st, 1st and 10th among 54 000 possible decoys. The results are further improved to 1st, 1st and 3rd when both DR and SIP filters are used. By applying only DR, a soluble system with distance restraints is recovered at the 1st-ranked pose. Availability and implementation https://github.com/capslockwizard/drsip. Supplementary information Supplementary data are available at Bioinformatics online.

HotSpot3D web server: an integrated resource for mutation analysis in protein 3D structures

2020 ◽  
Vol 36 (12) ◽  
pp. 3944-3946 ◽  
Author(s):  
Shanyu Chen ◽  
Xiaoyu He ◽  
Ruilin Li ◽  
Xiaohong Duan ◽  
Beifang Niu
Keyword(s):  
Mutation Analysis ◽  
Web Server ◽  
Cancer Genome ◽  
The Cancer Genome Atlas ◽  
Supplementary Information ◽  
Supplementary Data ◽  
3D Structures ◽  
One Stop ◽  
Cancer Genome Atlas ◽  
Genome Atlas

Abstract Motivation HotSpot3D is a widely used software for identifying mutation hotspots on the 3D structures of proteins. To further assist users, we developed a new HotSpot3D web server to make this software more versatile, convenient and interactive. Results The HotSpot3D web server performs data pre-processing, clustering, visualization and log-viewing on one stop. Users can interactively explore each cluster and easily re-visualize the mutational clusters within browsers. We also provide a database that allows users to search and visualize proximal mutations from 33 cancers in the Cancer Genome Atlas. Availability and implementation http://niulab.scgrid.cn/HotSpot3D/. Supplementary information Supplementary data are available at Bioinformatics online.

scholarly journals SEABED: Small molEcule activity scanner weB servicE baseD

2014 ◽  
Vol 31 (5) ◽  
pp. 773-775 ◽  
Author(s):  
Carlos Fenollosa ◽  
Marcel Otón ◽  
Pau Andrio ◽  
Jorge Cortés ◽  
Modesto Orozco ◽  
...  
Keyword(s):  
Web Service ◽  
Web Server ◽  
Software As A Service ◽  
Supplementary Information ◽  
Supplementary Data ◽  
Ensemble Docking ◽  
Web Tools ◽  
Protein Mutants ◽  
User Friendly ◽  
Hybrid Docking

Abstract Motivation: The SEABED web server integrates a variety of docking and QSAR techniques in a user-friendly environment. SEABED goes beyond the basic docking and QSAR web tools and implements extended functionalities like receptor preparation, library editing, flexible ensemble docking, hybrid docking/QSAR experiments or virtual screening on protein mutants. SEABED is not a monolithic workflow tool but Software as a Service platform. Availability and implementation: SEABED is a free web server available athttp://www.bsc.es/SEABED. No registration is required. Contact: [email protected] Supplementary information: Supplementary data are available atBioinformatics online.

scholarly journals Estimating the power of sequence covariation for detecting conserved RNA structure

2020 ◽  
Vol 36 (10) ◽  
pp. 3072-3076 ◽  
Author(s):  
Elena Rivas ◽  
Jody Clements ◽  
Sean R Eddy
Keyword(s):  
Secondary Structure ◽  
Sequence Alignment ◽  
Rna Structure ◽  
Rna Secondary Structure ◽  
Source Code ◽  
Web Server ◽  
Supplementary Information ◽  
Supplementary Data ◽  
Detection Power ◽  
Non Coding Rnas

Abstract Pairwise sequence covariations are a signal of conserved RNA secondary structure. We describe a method for distinguishing when lack of covariation signal can be taken as evidence against a conserved RNA structure, as opposed to when a sequence alignment merely has insufficient variation to detect covariations. We find that alignments for several long non-coding RNAs previously shown to lack covariation support do have adequate covariation detection power, providing additional evidence against their proposed conserved structures. Availability and implementation The R-scape web server is at eddylab.org/R-scape, with a link to download the source code. Supplementary information Supplementary data are available at Bioinformatics online.

scholarly journals IGLOSS: iterative gapless local similarity search

2019 ◽  
Vol 35 (18) ◽  
pp. 3491-3492
Author(s):  
Braslav Rabar ◽  
Maja Zagorščak ◽  
Strahil Ristov ◽  
Martin Rosenzweig ◽  
Pavle Goldstein
Keyword(s):  
Parameter Estimation ◽  
Similarity Search ◽  
Sequence Similarity ◽  
Web Server ◽  
Supplementary Information ◽  
Local Similarity ◽  
Supplementary Data ◽  
Matching Algorithm ◽  
Local Sequence ◽  
Sequence Patterns

Abstract Summary Searching for local sequence patterns is one of the basic tasks in bioinformatics. Sequence patterns might have structural, functional or some other relevance, and numerous methods have been developed to detect and analyze them. These methods often depend on the wealth of information already collected. The explosion in the number of newly available sequences calls for novel methods to explore local sequence similarity. We have developed a new method for iterative motif scanning that will look for ungapped sequence patterns similar to a submitted query. Using careful parameter estimation and an adaptation of a fast string-matching algorithm, the method performs significantly better in this context than the existing software. Availability and implementation The IGLOSS web server is available at http://compbioserv.math.hr/igloss/. Supplementary information Supplementary data are available at Bioinformatics online.

scholarly journals MMseqs2 desktop and local web server app for fast, interactive sequence searches

2019 ◽  
Vol 35 (16) ◽  
pp. 2856-2858 ◽  
Author(s):  
Milot Mirdita ◽  
Martin Steinegger ◽  
Johannes Söding
Keyword(s):  
Protein Sequence ◽  
Response Times ◽  
Web Server ◽  
Supplementary Information ◽  
Supplementary Data ◽  
Server Application ◽  
The Web

Abstract Summary The MMseqs2 desktop and web server app facilitates interactive sequence searches through custom protein sequence and profile databases on personal workstations. By eliminating MMseqs2’s runtime overhead, we reduced response times to a few seconds at sensitivities close to BLAST. Availability and implementation The app is easy to install for non-experts. GPLv3-licensed code, pre-built desktop app packages for Windows, MacOS and Linux, Docker images for the web server application and a demo web server are available at https://search.mmseqs.com. Supplementary information Supplementary data are available at Bioinformatics online.

scholarly journals m7GHub: deciphering the location, regulation and pathogenesis of internal mRNA N7-methylguanosine (m7G) sites in human

2020 ◽  
Vol 36 (11) ◽  
pp. 3528-3536 ◽  
Author(s):  
Bowen Song ◽  
Yujiao Tang ◽  
Kunqi Chen ◽  
Zhen Wei ◽  
Rong Rong ◽  
...  
Keyword(s):  
Recent Progress ◽  
Web Server ◽  
High Accuracy ◽  
Supplementary Information ◽  
Genetic Mutations ◽  
Supplementary Data ◽  
Rna Methylation ◽  
Online Platform ◽  
Main Components ◽  
The Impact

Abstract Motivation Recent progress in N7-methylguanosine (m7G) RNA methylation studies has focused on its internal (rather than capped) presence within mRNAs. Tens of thousands of internal mRNA m7G sites have been identified within mammalian transcriptomes, and a single resource to best share, annotate and analyze the massive m7G data generated recently are sorely needed. Results We report here m7GHub, a comprehensive online platform for deciphering the location, regulation and pathogenesis of internal mRNA m7G. The m7GHub consists of four main components, including: the first internal mRNA m7G database containing 44 058 experimentally validated internal mRNA m7G sites, a sequence-based high-accuracy predictor, the first web server for assessing the impact of mutations on m7G status, and the first database recording 1218 disease-associated genetic mutations that may function through regulation of m7G methylation. Together, m7GHub will serve as a useful resource for research on internal mRNA m7G modification. Availability and implementation m7GHub is freely accessible online at www.xjtlu.edu.cn/biologicalsciences/m7ghub. Contact [email protected] Supplementary information Supplementary data are available at Bioinformatics online.

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