Structure of the calcium-rich signature domain of human thrombospondin-2 View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2005-10

AUTHORS

C Britt Carlson, Douglas A Bernstein, Douglas S Annis, Tina M Misenheimer, Blue-leaf A Hannah, Deane F Mosher, James L Keck

ABSTRACT

Thrombospondins (THBSs) are secreted glycoproteins that have key roles in interactions between cells and the extracellular matrix. Here, we describe the 2.6-A-resolution crystal structure of the glycosylated signature domain of human THBS2, which includes three epidermal growth factor-like modules, 13 aspartate-rich repeats and a lectin-like module. These elements interact extensively to form three structural regions termed the stalk, wire and globe. The THBS2 signature domain is stabilized by these interactions and by a network of 30 bound Ca(2+) ions and 18 disulfide bonds. The structure suggests how genetic alterations of THBSs result in disease. More... »

PAGES

910-914

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsmb997

DOI

http://dx.doi.org/10.1038/nsmb997

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1031734770

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16186819


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