期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 12, 期 10, 页码 910-914出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb997
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资金
- NHLBI NIH HHS [T32 HL007899, HL54462, R01 HL054462, HL07899] Funding Source: Medline
- NIGMS NIH HHS [T32 GM008293, GM08293, T32 GM008692] Funding Source: Medline
Thrombospondins (THBSs) are secreted glycoproteins that have key roles in interactions between cells and the extracellular matrix. Here, we describe the 2.6-angstrom-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 Ca2+ ions and 18 disulfide bonds. The structure suggests how genetic alterations of THBSs result in disease.
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