1z78
Crystal Structure of the Thrombospondin-1 N-terminal domain
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OverviewOverview
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 A 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.
DiseaseDisease
Known disease associated with this structure: Sudden infant death with dysgenesis of the testes syndrome OMIM:[604714]
About this StructureAbout this Structure
1Z78 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
The structures of the thrombospondin-1 N-terminal domain and its complex with a synthetic pentameric heparin., Tan K, Duquette M, Liu JH, Zhang R, Joachimiak A, Wang JH, Lawler J, Structure. 2006 Jan;14(1):33-42. PMID:16407063
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