1ymw
From Proteopedia
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The study of reductive unfolding pathways of RNase A (Y92G mutant)
Overview
Reductive unfolding studies of proteins are designed to provide, information about intramolecular interactions that govern the formation, (and stabilization) of the native state and about folding/unfolding, pathways. By mutating Tyr92 to G, A, or L in the model protein, bovine, pancreatic ribonuclease A, and through analysis of temperature factors and, molecular dynamics simulations of the crystal structures of these mutants, it is demonstrated that the markedly different reductive unfolding rates, and pathways of ribonuclease A and its structural homologue onconase can, be attributed to a single, localized, ring-stacking interaction between, Tyr92 and Pro93 in the bovine variant. The fortuitous location of this, specific stabilizing interaction in a disulfide-bond-containing loop, region of ribonuclease A results in the localized modulation of protein, dynamics that, in turn, enhances the susceptibility of the disulfide bond, to reduction leading to an alteration in the reductive unfolding behavior, of the homologues. These results have important implications for folding, studies involving topological determinants to obtain folding/unfolding, rates and pathways, for protein structure-function prediction through fold, recognition, and for predicting proteolytic cleavage sites.
About this Structure
1YMW is a Single protein structure of sequence from Bos taurus. Active as Pancreatic ribonuclease, with EC number 3.1.27.5 Full crystallographic information is available from OCA.
Reference
A localized specific interaction alters the unfolding pathways of structural homologues., Xu G, Narayan M, Kurinov I, Ripoll DR, Welker E, Khalili M, Ealick SE, Scheraga HA, J Am Chem Soc. 2006 Feb 1;128(4):1204-13. PMID:16433537
Page seeded by OCA on Wed Nov 21 06:55:14 2007
