2ouh: Difference between revisions
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'''Crystal structure of the Thrombospondin-1 N-terminal domain in complex with fractionated Heparin DP10''' | {{Structure | ||
|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> | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= THBS1, TSP, TSP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Crystal structure of the Thrombospondin-1 N-terminal domain in complex with fractionated Heparin DP10''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2OUH is a [ | 2OUH is a [[Single protein]] structure of 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=2OUH OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/18065761 18065761] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tspn-1]] | [[Category: tspn-1]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:04:36 2008'' | ||
Revision as of 19:04, 20 March 2008
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| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , and | ||||||
| Ligands: | |||||||
| Gene: | THBS1, TSP, TSP1 (Homo sapiens) | ||||||
| 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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