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2erf

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Revision as of 19:38, 25 December 2014

Crystal Structure of the Thrombospondin-1 N-terminal Domain at 1.45A Resolution

Structural highlights

2erf is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1z78, 1za4
Gene:	THBS1, TSP, TSP1 (Homo sapiens)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[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.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Simantov R, Febbraio M, Crombie R, Asch AS, Nachman RL, Silverstein RL. Histidine-rich glycoprotein inhibits the antiangiogenic effect of thrombospondin-1. J Clin Invest. 2001 Jan;107(1):45-52. PMID:11134179 doi:http://dx.doi.org/10.1172/JCI9061
↑ Kvansakul M, Adams JC, Hohenester E. Structure of a thrombospondin C-terminal fragment reveals a novel calcium core in the type 3 repeats. EMBO J. 2004 Mar 24;23(6):1223-33. Epub 2004 Mar 11. PMID:15014436 doi:http://dx.doi.org/10.1038/sj.emboj.7600166
↑ Tan K, Duquette M, Liu JH, Zhang R, Joachimiak A, Wang JH, Lawler J. The structures of the thrombospondin-1 N-terminal domain and its complex with a synthetic pentameric heparin. Structure. 2006 Jan;14(1):33-42. PMID:16407063 doi:10.1016/j.str.2005.09.017

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2erf"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2erf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ERF FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1z78|1z78]], [[1za4|1za4]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1z78|1z78]], [[1za4|1za4]]</td></tr>
-<tr><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 Homo sapiens])</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 Homo sapiens])</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2erf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2erf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2erf RCSB], [http://www.ebi.ac.uk/pdbsum/2erf PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2erf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2erf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2erf RCSB], [http://www.ebi.ac.uk/pdbsum/2erf PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 32: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Lawler, J.]]
+[[Category: Lawler, J]]
-[[Category: Tan, K.]]
+[[Category: Tan, K]]
-[[Category: Wang, J.]]
+[[Category: Wang, J]]
 [[Category: Hbd]]
 [[Category: N-terminal tspn]]

2erf

From Proteopedia

Revision as of 19:38, 25 December 2014

Crystal Structure of the Thrombospondin-1 N-terminal Domain at 1.45A Resolution

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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