1Z78
Crystal Structure of the Thrombospondin-1 N-terminal domain
Summary for 1Z78
| Entry DOI | 10.2210/pdb1z78/pdb |
| Descriptor | Thrombospondin 1 (2 entities in total) |
| Functional Keywords | tsp-1, ntsp-1, cell adhesion |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 23598.80 |
| Authors | Tan, K.,Wang, J.,Lawler, J. (deposition date: 2005-03-24, release date: 2006-01-17, Last modification date: 2024-11-20) |
| Primary citation | Tan, K.,Duquette, M.,Liu, J.H.,Zhang, R.,Joachimiak, A.,Wang, J.H.,Lawler, J. The structures of the thrombospondin-1 N-terminal domain and its complex with a synthetic pentameric heparin. Structure, 14:33-42, 2006 Cited by PubMed Abstract: 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. PubMed: 16407063DOI: 10.1016/j.str.2005.09.017 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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