Functional Analysis of the Chitin-binding Domain of a Family 19 Chitinase fromStreptomyces griseusHUT6037: Substrate-binding Affinity andcis-Dominant Increase of Antifungal Function

2002 ◽  
Vol 66 (5) ◽  
pp. 1084-1092 ◽  
Author(s):  
Yoshikane ITOH ◽  
Tomokazu KAWASE ◽  
Naoki NIKAIDOU ◽  
Harumi FUKADA ◽  
Masaru MITSUTOMI ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Binding Affinity ◽  
Substrate Binding ◽  
Binding Domain ◽  
Chitin Binding Domain ◽  
Family 19 Chitinase

Swapping the chitin-binding domain in Bacillus chitinases improves the substrate binding affinity and conformational stability

2010 ◽  
Vol 6 (8) ◽  
pp. 1492 ◽  
Author(s):  
Chilukoti Neeraja ◽  
Rajagopal Subramanyam ◽  
Bruno M. Moerschbacher ◽  
Appa Rao Podile
Keyword(s):  
Binding Affinity ◽  
Substrate Binding ◽  
Conformational Stability ◽  
Binding Domain ◽  
Chitin Binding Domain

CLONING AND EXPRESSION OF CHITINASE 19 FAMILIE FROM D.CAPENSIS

2020 ◽  
pp. 288-290
Author(s):  
A. Chulkin ◽  
A. Rozhkova ◽  
A. Sinitsyn A.
Keyword(s):  
Binding Domain ◽  
Full Length ◽  
Cloning And Expression ◽  
Chitin Binding Domain ◽  
Biochemical Characteristics ◽  
Family 19 Chitinase ◽  
Different Strains

Sequence of family 19 chitinase was cloned from Drosera capensis. Implemented expression in different strains of E.coli and developed a refolding method. Describes the primary biochemical characteristics of the full-length chitinase and its shape without chitin-binding domain.

Distinct Modulation of Wild-Type and Selective Gene Mutated Vitamin D Receptor by Essential Poly Unsaturated Fatty Acids

2021 ◽  
Vol 21 ◽  
Author(s):  
Hari Balaji ◽  
Selvaraj Ayyamperuma ◽  
Niladri Saha ◽  
Shyam Sundar Pottabathula ◽  
Jubie Selvaraj ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Vitamin D ◽  
Ligand Binding ◽  
Vitamin D Deficiency ◽  
Binding Affinity ◽  
Unsaturated Fatty Acids ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Binding Energies ◽  
Wild Type

: Vitamin-D deficiency is a global concern. Gene mutations in the vitamin D receptor’s (VDR) ligand binding domain (LBD) variously alter the ligand binding affinity, heterodimerization with retinoid X receptor (RXR) and inhibit coactivator interactions. These LBD mutations may result in partial or total hormone unresponsiveness. A plethora of evidence report that selective long chain polyunsaturated fatty acids (PUFAs) including eicosapentaenoic acid (EPA), docosahexaenoic acid (DHA) and arachidonic acid (AA) bind to the ligand-binding domain of VDR and lead to transcriptional activation. We therefore hypothesize that selective PUFAs would modulate the dynamics and kinetics of VDRs, irrespective bioactive of vitamin-D binding. The spatial arrangements of the selected PUFAs in VDR active site were examined by in-silico docking studies. The docking results revealed that PUFAs have fatty acid structure-specific binding affinity towards VDR. The calculated EPA, DHA & AA binding energies (Cdocker energy) were lesser compared to vitamin-D in wild type of VDR (PDB id: 2ZLC). Of note, the DHA has higher binding interactions to the mutated VDR (PDB id: 3VT7) when compared to the standard Vitamin-D. Molecular dynamic simulation was utilized to confirm the stability of potential compound binding of DHA with mutated VDR complex. These findings suggest the unique roles of PUFAs in VDR activation and may offer alternate strategy to circumvent vitamin-D deficiency.

scholarly journals Entropic Inhibition: How the Activity of a AAA+ Machine Is Modulated by Its Substrate-Binding Domain

2021 ◽  
Author(s):  
Marija Iljina ◽  
Hisham Mazal ◽  
Pierre Goloubinoff ◽  
Inbal Riven ◽  
Gilad Haran
Keyword(s):  
Substrate Binding ◽  
Binding Domain ◽  
Substrate Binding Domain

scholarly journals Flexible Linkers Leash the Substrate Binding Domain of SspB to a Peptide Module that Stabilizes Delivery Complexes with the AAA+ ClpXP Protease

2003 ◽  
Vol 12 (2) ◽  
pp. 355-363 ◽  
Author(s):  
David A Wah ◽  
Igor Levchenko ◽  
Gabrielle E Rieckhof ◽  
Daniel N Bolon ◽  
Tania A Baker ◽  
...  
Keyword(s):  
Substrate Binding ◽  
Binding Domain ◽  
Substrate Binding Domain
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