1z78

<table><tr><td colspan='2'>[[1z78]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z78 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Z78 FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">THBS1, TSP, TSP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1z78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z78 OCA], [http://pdbe.org/1z78 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z78 RCSB], [http://www.ebi.ac.uk/pdbsum/1z78 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z78 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/TSP1_HUMAN TSP1_HUMAN]] Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Binds heparin. May play a role in dentinogenesis and/or maintenance of dentin and dental pulp (By similarity). Ligand for CD36 mediating antiangiogenic properties.<ref>PMID:11134179</ref> <ref>PMID:15014436</ref>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:16407063</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1z78" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Lawler, J]]

[[Category: Tan, K]]

[[Category: Wang, J]]

[[Category: Tsp-1]]