Chemical specificity and conformational flexibility in proteinase-inhibitor interaction: Scaffolds for promiscuous binding

Vishwanath, Sneha and Srinivasan, Narayanaswamy (2014) Chemical specificity and conformational flexibility in proteinase-inhibitor interaction: Scaffolds for promiscuous binding. In: PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY, 116 (2-3). pp. 151-157.

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Abstract

One of the most important roles of proteins in cellular milieu is recognition of other biomolecules including other proteins. Protein protein complexes are involved in many essential cellular processes. Interfaces of protein protein complexes are traditionally known to be conserved in evolution and less flexible than other solvent interacting tertiary structural surface. But many examples are emerging where these features do not hold good. An understanding of inter-play between flexibility and sequence conservation is emerging, providing a fresh dimension to the paradigm of sequence structure function relationship. The functional manifestation of the inter-relation between sequence conservation and flexibility of interface is exemplified in this review using proteinase inhibitor protein complexes. (C) 2014 Elsevier Ltd. All rights reserved.

Item Type:	Journal Article
Publication:	PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY
Publisher:	PERGAMON-ELSEVIER SCIENCE LTD
Additional Information:	Copy right for this article belongs to the PERGAMON-ELSEVIER SCIENCE LTD, THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND
Keywords:	Interface flexibility; Promiscuous binding; Proteinases; Proteinase inhibitors; Protein-protein interaction; Sequence variability
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	06 Feb 2015 14:58
Last Modified:	06 Feb 2015 14:58
URI:	http://eprints.iisc.ac.in/id/eprint/50786

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