Anion induced conformational preference of CαNN motif residues in functional proteins
| Autor: | Jaydeb Chakrabarti, Mahua Ghosh, Raja Banerjee, Piya Patra |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Peptide fragment Stereochemistry Chemistry 010402 general chemistry 01 natural sciences Biochemistry 0104 chemical sciences Ion 03 medical and health sciences Molecular dynamics Crystallography 030104 developmental biology Peptide backbone Sequence dependent Structural Biology Motif (music) Anion binding Molecular Biology Protein secondary structure |
| Zdroj: | Proteins: Structure, Function, and Bioinformatics. 85:2179-2190 |
| ISSN: | 0887-3585 |
| Popis: | Among different ligand binding motifs, anion binding CαNN motif consisting of peptide backbone atoms of three consecutive residues are observed to be important for recognition of free anions, like sulphate or bi-phosphate and participate in different key functions. Here we study the interaction of sulphate and bi-phosphate with CαNN motif present in different proteins. Instead of total protein, a peptide fragment has been studied keeping CαNN motif flanked in between other residues. We use classical force field based Molecular Dynamics Simulations to understand the stability of this motif. Our data indicate fluctuations in conformational preferences of the motif residues in absence of the anion. The anion gives stability to one of these conformations. However, the anion induced conformational preferences are highly sequence dependent and specific to the type of anion. In particular the polar residues are more favourable compared to the other residues for recognising the anion. This article is protected by copyright. All rights reserved. |
| Databáze: | OpenAIRE |
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