Comparison of tertiary structures of proteins in protein-protein complexes with unbound forms suggests prevalence of allostery in signalling proteins.

BMC Structural Biology
Lakshmipuram S SwapnaNarayanaswamy Srinivasan

Abstract

Most signalling and regulatory proteins participate in transient protein-protein interactions during biological processes. They usually serve as key regulators of various cellular processes and are often stable in both protein-bound and unbound forms. Availability of high-resolution structures of their unbound and bound forms provides an opportunity to understand the molecular mechanisms involved. In this work, we have addressed the question "What is the nature, extent, location and functional significance of structural changes which are associated with formation of protein-protein complexes?" A database of 76 non-redundant sets of high resolution 3-D structures of protein-protein complexes, representing diverse functions, and corresponding unbound forms, has been used in this analysis. Structural changes associated with protein-protein complexation have been investigated using structural measures and Protein Blocks description. Our study highlights that significant structural rearrangement occurs on binding at the interface as well as at regions away from the interface to form a highly specific, stable and functional complex. Notably, predominantly unaltered interfaces interact mainly with interfaces undergoing substantial str...Continue Reading

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Citations

Jan 8, 2016·Chemical Reviews·Andre A S T Ribeiro, Vanessa Ortiz
Nov 26, 2015·IUCrJ·Devlina ChakravartyPinak Chakrabarti
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May 15, 2020·Journal of Bioinformatics and Computational Biology·Muthuvel Prasath KaruppasamyParthasarathy Subbiah

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Methods Mentioned

BETA
two-hybrid
X-ray
RSA
GTPase
nucleotide exchange
nucleotide
PISA

Software Mentioned

ProtCID
iPfam
Complex
PBSSc
oGNM
GNM
PyMOL
NACCESS
SNAPPI
DB

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