Ontology highlight
ABSTRACT:
SUBMITTER: Calzada MJ
PROVIDER: S-EPMC2442560 | biostudies-literature | 2008 May
REPOSITORIES: biostudies-literature
Calzada Maria J MJ Kuznetsova Svetlana A SA Sipes John M JM Rodrigues Rui G RG Cashel Jo Anne JA Annis Douglas S DS Mosher Deane F DF Roberts David D DD
Matrix biology : journal of the International Society for Matrix Biology 20071215 4
Conformational changes induced in thrombospondin-1 by removal of calcium regulate interactions with some ligands of its N-modules. Because calcium binds primarily to elements of the C-terminal signature domain of thrombospondin-1, which are distant from the N-modules, such regulation was unexpected. To clarify the mechanism for this regulation, we compared ligand binding to the N-modules of thrombospondin-1 in the full-length protein and recombinant trimeric thrombospondin-1 truncated prior to t ...[more]