Global distribution of conformational states derived from redundant models in the PDB points to non-uniqueness of the protein structure.

ABSTRACT: It is commonly accepted that proteins have evolutionarily conserved 3-dimensional structures, uniquely defined by their amino acid sequence. Here, we question the direct association of structure to sequence by comparing multiple models of identical proteins. Rapidly growing structural databases contain models of proteins determined independently multiple times. We have collected these models in the database of the redundant sets of protein structures and then derived their conformational states by clustering the models with low root-mean-square deviations (RMSDs). The distribution of conformational states represented in these sets is wider than commonly believed, in fact exceeding the possible range of structure determination errors, by at least an order of magnitude. We argue that differe

SUBMITTER: Burra PV 

PROVIDER: S-EPMC2705611 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature