期刊
STRUCTURE
卷 14, 期 1, 页码 33-42出版社
CELL PRESS
DOI: 10.1016/j.str.2005.09.017
关键词
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资金
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL068003, R01HL049081] Funding Source: NIH RePORTER
- NHLBI NIH HHS [R01 HL049081-07, R01 HL068003, HL68003, R01 HL068003-04, R01 HL049081-09, R01 HL049081, HL49081] Funding Source: Medline
The N-terminal domain of thrombospondin-1 (TSPN-1) mediates the protein's interaction with (1) glycosaminoglycans, calreticulin, and integrins during cellular adhesion, (2) low-density lipoprotein receptor-related protein during uptake and clearance, and (3) fibrinogen during platelet aggregation. The crystal structure of TSPN-1 to 1.8 angstrom resolution is a beta sandwich with 13 antiparallel beta strands and 1 irregular strand-like segment. Unique structural features of the N- and C-terminal regions, and the disulfide bond location, distinguish TSPN-1 from the laminin G domain and other concanavalin A-like lectins/glucanases superfamily members. The crystal structure of the complex of TSPN-1 with heparin indicates that residues R29, R42, and R77 in an extensive positively charged patch at the bottom of the domain specifically associate with the sulfate groups of heparin. The TSPN-1 structure and identified adjacent linker region provide a structural framework for the analysis of the TSPN domain of various molecules, including TSPs, NELLs, many collagens, TSPEAR, and kielin.
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