scholarly journals Evidence that the TRPV1 S1-S4 Membrane Domain Contributes to Thermosensing

2019 ◽  
Author(s):  
Minjoo Kim ◽  
Nicholas J. Sisco ◽  
Jacob K. Hilton ◽  
Camila M. Montano ◽  
Manuel A. Castro ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Solution Nmr ◽  
Membrane Domain ◽  
Temperature Dependent ◽  
Nmr Characterization ◽  
Significant Interest ◽  
Pore Domain ◽  
Coupling Mechanisms

AbstractSensing and responding to temperature is crucial in biology. The TRPV1 ion channel is a well-studied heat-sensing receptor that is also activated by vanilloid compounds including capsaicin. Despite significant interest, the molecular underpinnings of thermosensing have remained elusive. The TRPV1 S1-S4 membrane domain couples chemical ligand binding to the pore domain during channel gating. However, the role of the S1-S4 domain in thermosensing is unclear. Evaluation of the isolated human TRPV1 S1-S4 domain by solution NMR, Far-UV CD, and intrinsic fluorescence shows that this domain undergoes a non-denaturing temperature-dependent transition with a high thermosensitivity. Further NMR characterization of the temperature-dependent conformational changes suggests the contribution of the S1-S4 domain to thermosensing shares features with known coupling mechanisms between this domain with ligand and pH activation. Taken together, this study shows that the TRPV1 S1-S4 domain contributes to TRPV1 temperature-dependent activation.

Approaches to the Solution NMR Characterization of Active Sites for 65 kDa Tetrameric Hemoglobins in the Paramagnetic Cyanomet State

1997 ◽  
Vol 119 (51) ◽  
pp. 12643-12654 ◽  
Author(s):  
Urszula Kolczak ◽  
Chang Han ◽  
L. A. Sylvia ◽  
Gerd N. La Mar
Keyword(s):  
Active Sites ◽  
Solution Nmr ◽  
Nmr Characterization

scholarly journals Solution NMR characterization of chemokine CXCL8/IL-8 monomer and dimer binding to glycosaminoglycans: structural plasticity mediates differential binding interactions

2015 ◽  
Vol 472 (1) ◽  
pp. 121-133 ◽  
Author(s):  
Prem Raj B. Joseph ◽  
Philip D. Mosier ◽  
Umesh R. Desai ◽  
Krishna Rajarathnam
Keyword(s):  
Structural Plasticity ◽  
Neutrophil Function ◽  
Solution Nmr ◽  
Binding Interactions ◽  
High Affinity ◽  
Nmr Characterization ◽  
Differential Binding

Structural plasticity plays a major role in determining differential binding of CXCL8 monomer and dimer to glycosaminoglycans (GAGs) and that dimer is the high-affinity GAG ligand. We propose that these properties play important roles in orchestrating in vivo chemokine-mediated neutrophil function.

Advanced solid-state 1H/31P NMR characterization of pyrophosphate-doped calcium phosphate cements for biomedical applications: The structural role of pyrophosphate

2019 ◽  
Vol 45 (16) ◽  
pp. 20642-20655 ◽  
Author(s):  
Yang Yu ◽  
Hua Guo ◽  
Michael Pujari-Palmer ◽  
Baltzar Stevensson ◽  
Jekabs Grins ◽  
...  
Keyword(s):  
Solid State ◽  
Calcium Phosphate ◽  
Biomedical Applications ◽  
31P Nmr ◽  
Structural Role ◽  
Calcium Phosphate Cements ◽  
Nmr Characterization

Solution NMR characterization of apical membrane antigen 1 and small molecule interactions as a basis for designing new antimalarials

2016 ◽  
Vol 29 (6) ◽  
pp. 281-291 ◽  
Author(s):  
Bankala Krishnarjuna ◽  
San Sui Lim ◽  
Shane M. Devine ◽  
Cael O. Debono ◽  
Raymond Lam ◽  
...  
Keyword(s):  
Small Molecule ◽  
Apical Membrane ◽  
Solution Nmr ◽  
Apical Membrane Antigen 1 ◽  
Apical Membrane Antigen ◽  
Nmr Characterization ◽  
Molecule Interactions

Solution NMR characterization of Sgf73(1–104) indicates that Zn ion is required to stabilize zinc finger motif

2010 ◽  
Vol 397 (3) ◽  
pp. 436-440 ◽  
Author(s):  
Chaohua Lai ◽  
Minhao Wu ◽  
Pan Li ◽  
Chaowei Shi ◽  
Changlin Tian ◽  
...  
Keyword(s):  
Zinc Finger ◽  
Solution Nmr ◽  
Zinc Finger Motif ◽  
Nmr Characterization

scholarly journals Role of the S3-S4 Linker in Shaker Potassium Channel Activation

1997 ◽  
Vol 109 (2) ◽  
pp. 191-199 ◽  
Author(s):  
Rajesh Mathur ◽  
Jie Zheng ◽  
Yangyang Yan ◽  
Fred J. Sigworth
Keyword(s):  
Conformational Changes ◽  
Xenopus Oocytes ◽  
Channel Activation ◽  
Activation Kinetics ◽  
Shaker Potassium Channel ◽  
Large Conformational Change ◽  
Voltage Gated Channels ◽  
Mutant Construct

Structural models of voltage-gated channels suggest that flexibility of the S3-S4 linker region may be important in allowing the S4 region to undergo large conformational changes in its putative voltage-sensing function. We report here the initial characterization of 18 mutations in the S3-S4 linker of the Shaker channel, including deletions, insertions, charge changes, substitution of prolines, and chimeras replacing the 25-residue Shaker linker with 7- or 9-residue sequences from Shab, Shaw, or Shal. As measured in Xenopus oocytes with a two-microelectrode voltage clamp, each mutant construct yielded robust currents. Changes in the voltage dependence of activation were small, with activation voltage shifts of 13 mV or less. Substitution of linkers from the slowly activating Shab and Shaw channels resulted in a three- to fourfold slowing of activation and deactivation. It is concluded that the S3-S4 linker is unlikely to participate in a large conformational change during channel activation. The linker, which in some channel subfamilies has highly conserved sequences, may however be a determinant of activation kinetics in potassium channels, as previously has been suggested in the case of calcium channels.

scholarly journals NMR Characterization of the Interactions Between Glycosaminoglycans and Proteins

2021 ◽  
Vol 8 ◽  
Author(s):  
Changkai Bu ◽  
Lan Jin
Keyword(s):  
Protein Interactions ◽  
Dimensional Space ◽  
Three Dimensional ◽  
Gag Protein ◽  
Physiological Processes ◽  
Nmr Characterization ◽  
Mammalian Tissues ◽  
Three Dimensional Space

Glycosaminoglycans (GAGs) constitute a considerable fraction of the glycoconjugates found on cellular membranes and in the extracellular matrix of virtually all mammalian tissues. The essential role of GAG-protein interactions in the regulation of physiological processes has been recognized for decades. However, the underlying molecular basis of these interactions has only emerged since 1990s. The binding specificity of GAGs is encoded in their primary structures, but ultimately depends on how their functional groups are presented to a protein in the three-dimensional space. This review focuses on the application of NMR spectroscopy on the characterization of the GAG-protein interactions. Examples of interpretation of the complex mechanism and characterization of structural motifs involved in the GAG-protein interactions are given. Selected families of GAG-binding proteins investigated using NMR are also described.

NMR Characterization of the Metallo-β-lactamase fromBacteroides fragilisand Its Interaction with a Tight-Binding Inhibitor:  Role of an Active-Site Loop†

Biochemistry ◽  
1999 ◽  
Vol 38 (44) ◽  
pp. 14507-14514 ◽  
Author(s):  
Sergio D. B. Scrofani ◽  
John Chung ◽  
James J. A. Huntley ◽  
Stephen J. Benkovic ◽  
Peter E. Wright ◽  
...  
Keyword(s):  
Active Site ◽  
Tight Binding ◽  
Nmr Characterization

Solution NMR Characterization of the Thermodynamics of the Disulfide Bond Orientational Isomerism and Its Effect of Cluster Electronic Properties for the Hyperthermostable Three-Iron Cluster Ferredoxin from the ArchaeonPyrococcus furiosus†

Biochemistry ◽  
2001 ◽  
Vol 40 (42) ◽  
pp. 12575-12583 ◽  
Author(s):  
Mateus Webba da Silva ◽  
Simon Sham ◽  
Carol M. Gorst ◽  
Luigi Calzolai ◽  
Philip S. Brereton ◽  
...  
Keyword(s):  
Electronic Properties ◽  
Disulfide Bond ◽  
Solution Nmr ◽  
Iron Cluster ◽  
Nmr Characterization

17O Solution NMR Characterization of the Preparation of Sol−Gel Derived SiO2/TiO2and SiO2/ZrO2Glasses

1997 ◽  
Vol 9 (11) ◽  
pp. 2385-2394 ◽  
Author(s):  
Laurent Delattre ◽  
Florence Babonneau
Keyword(s):  
Sol Gel ◽  
Solution Nmr ◽  
Nmr Characterization
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