Traditional biomolecular structure determination by NMR spectroscopy allows for major errors.

ABSTRACT: One of the major goals of structural genomics projects is to determine the three-dimensional structure of representative members of as many different fold families as possible. Comparative modeling is expected to fill the remaining gaps by providing structural models of homologs of the experimentally determined proteins. However, for such an approach to be successful it is essential that the quality of the experimentally determined structures is adequate. In an attempt to build a homology model for the protein dynein light chain 2A (DLC2A) we found two potential templates, both experimentally determined nuclear magnetic resonance (NMR) structures originating from structural genomics efforts. Despite their high sequence identity (96%), the folds of the two structures are markedly different.

SUBMITTER: Nabuurs SB 

PROVIDER: S-EPMC1359070 | biostudies-literature | 2006 Feb

REPOSITORIES: biostudies-literature