Object's details: Halogen bonding at the ATP binding site of protein kinases: preferred geometry and topology of ligand binding.

Provider:Repozytorium Instytutu Biochemii i Biofizyki Polskiej Akademii Nauk

Description

Title:
Halogen bonding at the ATP binding site of protein kinases: preferred geometry and topology of ligand binding.
Creator:
Poznański, Jarosław;
Shugar, David
Description:
Halogenated ligands have been widely developed as potent, and frequently selective, inhibitors of protein kinases (PK). Herein, all structures of protein kinases complexed with a halogenated ligand, identified in the PDB, were analyzed in the context of eventual contribution of halogen bonding to protein-ligand interactions. Global inspection shows that two carbonyl groups of residues located in the hinge region are the most abundant halogen bond acceptors. In contrast to solution data, well-defined water molecules, located at sites conserved across most PK structures, are also involved in halogen bonding. Analysis of cumulative distributions of halogen-acceptor distances shows that structures displaying short contacts involving a halogen atom are overpopulated, contributing together to clearly defined maxima of 2.82, 2.91 and 2.94Å for chlorine, bromine and iodine, respectively. The angular preference of a halogen bond favors ideal topology (180°, 120°) for iodine. For bromine the distribution is much more dispersed, and no such preference was found for chlorine. This article is part of a Special Issue entitled: Inhibitors of Protein Kinases (2012).
Object availability:
free access
Date:
2013.07
Type:
Article;
PeerReviewed
Language:
English
Format:
application/pdf
Publisher:
Elsevier
Relation: http://eprints.ibb.waw.pl/635 ;http://www.sciencedirect.com/science/article/pii/S157096391300037X ;
10.1016/j.bbapap.2013.01.026
Subject:
Q Science (General);
QD Chemistry
Identifier: http://eprints.ibb.waw.pl/635/1/BBA-121221h.pdf ;
Poznański, Jarosław and Shugar, David (2013) Halogen bonding at the ATP binding site of protein kinases: preferred geometry and topology of ligand binding. Biochimica et Biophysica Acta, 1834 (7). pp. 1381-6. ISSN 10-1016
Data provider:
Repozytorium Instytutu Biochemii i Biofizyki Polskiej Akademii Nauk

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Object's details: Halogen bonding at the ATP binding site of protein kinases: preferred geometry and topology of ligand binding.

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