Ontology highlight
ABSTRACT:
SUBMITTER: Walters RF
PROVIDER: S-EPMC1564267 | biostudies-literature | 2006 Sep
REPOSITORIES: biostudies-literature
Walters R F S RF DeGrado W F WF
Proceedings of the National Academy of Sciences of the United States of America 20060905 37
The fold of a helical membrane protein is largely determined by interactions between membrane-imbedded helices. To elucidate recurring helix-helix interaction motifs, we dissected the crystallographic structures of membrane proteins into a library of interacting helical pairs. The pairs were clustered according to their three-dimensional similarity (rmsd </=1.5 A), allowing 90% of the library to be assigned to clusters consisting of at least five members. Surprisingly, three quarters of the heli ...[more]