Structures of an unliganded neurophysin and its vasopressin complex: implications for binding and allosteric mechanisms.

ABSTRACT: The structures of des 1-6 bovine neurophysin-II in the unliganded state and as its complex with lysine vasopressin were determined crystallographically at resolutions of 2.4 A and 2.3 A, respectively. The structure of the protein component of the vasopressin complex was, with some local differences, similar to that determined earlier of the full-length protein complexed with oxytocin, but relatively large differences, probably intrinsic to the hormones, were observed between the structures of bound oxytocin and bound vasopressin at Gln 4. The structure of the unliganded protein is the first structure of an unliganded neurophysin. Comparison with the liganded state indicated significant binding-induced conformational changes that were the largest in the loop region comprising residues 50-58

SUBMITTER: Wu CK 

PROVIDER: S-EPMC2253203 | biostudies-literature | 2001 Sep

REPOSITORIES: biostudies-literature