2ouh: Difference between revisions
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|PDB= 2ouh |SIZE=350|CAPTION= <scene name='initialview01'>2ouh</scene>, resolution 2.4Å | |PDB= 2ouh |SIZE=350|CAPTION= <scene name='initialview01'>2ouh</scene>, resolution 2.4Å | ||
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Residue+A+248'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Residue+A+249'>AC2</scene>, <scene name='pdbsite=AC3:So4+Binding+Site+For+Residue+A+250'>AC3</scene>, <scene name='pdbsite=AC4:So4+Binding+Site+For+Residue+B+248'>AC4</scene>, <scene name='pdbsite=AC5:So4+Binding+Site+For+Residue+B+249'>AC5</scene> and <scene name='pdbsite=AC6:So4+Binding+Site+For+Residue+B+250'>AC6</scene> | |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Residue+A+248'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Residue+A+249'>AC2</scene>, <scene name='pdbsite=AC3:So4+Binding+Site+For+Residue+A+250'>AC3</scene>, <scene name='pdbsite=AC4:So4+Binding+Site+For+Residue+B+248'>AC4</scene>, <scene name='pdbsite=AC5:So4+Binding+Site+For+Residue+B+249'>AC5</scene> and <scene name='pdbsite=AC6:So4+Binding+Site+For+Residue+B+250'>AC6</scene> | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= THBS1, TSP, TSP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= THBS1, TSP, TSP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1z78|1Z78]], [[1za4|1ZA4]], [[2ouj|2OUJ]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ouh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ouh OCA], [http://www.ebi.ac.uk/pdbsum/2ouh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ouh RCSB]</span> | |||
}} | }} | ||
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[[Category: Tan, K.]] | [[Category: Tan, K.]] | ||
[[Category: Wang, J.]] | [[Category: Wang, J.]] | ||
[[Category: cell adhesion]] | [[Category: cell adhesion]] | ||
[[Category: dp10]] | [[Category: dp10]] | ||
| Line 34: | Line 36: | ||
[[Category: tspn-1]] | [[Category: tspn-1]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:23:16 2008'' | ||
Revision as of 04:23, 31 March 2008
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| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , and | ||||||
| Ligands: | |||||||
| Gene: | THBS1, TSP, TSP1 (Homo sapiens) | ||||||
| Related: | 1Z78, 1ZA4, 2OUJ
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the Thrombospondin-1 N-terminal domain in complex with fractionated Heparin DP10
OverviewOverview
Through its interactions with proteins and proteoglycans, thrombospondin-1 (TSP-1) functions at the interface of the cell membrane and the extracellular matrix to regulate matrix structure and cellular phenotype. We have previously determined the structure of the high affinity heparin-binding domain of TSP-1, designated TSPN-1, in association with the synthetic heparin, Arixtra. To establish that the binding of TSPN-1 to Arixtra is representative of the association with naturally occurring heparins, we have determined the structures of TSPN-1 in complex with heparin oligosaccharides containing eight (dp8) and ten (dp10) subunits, by x-ray crystallography. We have found that dp8 and dp10 bind to TSPN-1 in a manner similar to Arixtra and that dp8 and dp10 induce the formation of trans and cis TSPN-1 dimers, respectively. In silico docking calculations partnered with our crystal structures support the importance of arginine residues in positions 29, 42, and 77 in binding sulfate groups of the dp8 and dp10 forms of heparin. The ability of several TSPN-1 domains to bind to glycosaminoglycans simultaneously probably increases the affinity of binding through multivalent interactions. The formation of cis and trans dimers of the TSPN-1 domain with relatively short segments of heparin further enhances the ability of TSP-1 to participate in high affinity binding to glycosaminoglycans. Dimer formation may also involve TSPN-1 domains from two separate TSP-1 molecules. This association would enable glycosaminoglycans to cluster TSP-1.
About this StructureAbout this Structure
2OUH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Heparin-induced cis- and trans-Dimerization Modes of the Thrombospondin-1 N-terminal Domain., Tan K, Duquette M, Liu JH, Shanmugasundaram K, Joachimiak A, Gallagher JT, Rigby AC, Wang JH, Lawler J, J Biol Chem. 2008 Feb 15;283(7):3932-41. Epub 2007 Dec 7. PMID:18065761
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