Interactions among the epidermal growth factor-like modules of thrombospondin-1.

ABSTRACT: Epidermal growth factor (EGF)-like modules are defined in part by six cysteines joined by disulfides in a 1-3, 2-4, and 5-6 pattern. Thrombospondin-1 (TSP-1) is a multimodular glycoprotein with three EGF-like modules, E1, E2, and E3, arranged in tandem. These modules likely propagate conformational changes between surrounding C-terminal and N-terminal elements of TSP-1 and interact with other extracellular molecules. E1, E2, and their homologs in other TSPs are unique among EGF-like modules in having two residues rather than one between Cys-4 and Cys-5. In addition, E2 has a calcium-binding site and an unusually long loop between Cys-5 and Cys-6. The structure of E1, E2, or E3 expressed alone changed little upon heating as monitored by far-UV CD, whereas more marked changes occurred in E12

SUBMITTER: Liu Y 

PROVIDER: S-EPMC2755945 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature