Identification of amino acids that account for long-range interactions in two triosephosphate isomerases from pathogenic trypanosomes.

ABSTRACT: For a better comprehension of the structure-function relationship in proteins it is necessary to identify the amino acids that are relevant for measurable protein functions. Because of the numerous contacts that amino acids establish within proteins and the cooperative nature of their interactions, it is difficult to achieve this goal. Thus, the study of protein-ligand interactions is usually focused on local environmental structural differences. Here, using a pair of triosephosphate isomerase enzymes with extremely high homology from two different organisms, we demonstrate that the control of a seventy-fold difference in reactivity of the interface cysteine is located in several amino acids from two structurally unrelated regions that do not contact the cysteine sensitive to the sulfhydry

SUBMITTER: Garcia-Torres I 

PROVIDER: S-EPMC3078909 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature