2ouj: Difference between revisions

Revision as of 18:45, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ouj.png

Template:STRUCTURE 2ouj

The crystal structure of the Thrombospondin-1 N-terminal domain in complex with fractionated Heparin DP8The crystal structure of the Thrombospondin-1 N-terminal domain in complex with fractionated Heparin DP8

Template:ABSTRACT PUBMED 18065761

About this StructureAbout this Structure

2OUJ 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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''The crystal structure of the Thrombospondin-1 N-terminal domain in complex with fractionated Heparin DP8'''
+===The crystal structure of the Thrombospondin-1 N-terminal domain in complex with fractionated Heparin DP8===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_18065761}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18065761 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_18065761}}
 ==About this Structure==
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 [[Category: Tsp-1]]
 [[Category: Tspn-1]]
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