2hyw

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[[Image:2hyw.jpg|left|200px]]
[[Image:2hyw.jpg|left|200px]]
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{{Structure
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|PDB= 2hyw |SIZE=350|CAPTION= <scene name='initialview01'>2hyw</scene>, resolution 2.100&Aring;
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The line below this paragraph, containing "STRUCTURE_2hyw", creates the "Structure Box" on the page.
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|SITE=
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|GENE= ANXA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_2hyw| PDB=2hyw | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hyw OCA], [http://www.ebi.ac.uk/pdbsum/2hyw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hyw RCSB]</span>
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'''Human Annexin A2 with Calcium bound'''
'''Human Annexin A2 with Calcium bound'''
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[[Category: Seaton, B A.]]
[[Category: Seaton, B A.]]
[[Category: Shao, C.]]
[[Category: Shao, C.]]
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[[Category: calcium-binding protein]]
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[[Category: Calcium-binding protein]]
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[[Category: helix bundle]]
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[[Category: Helix bundle]]
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[[Category: membrane-binding protein]]
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[[Category: Membrane-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:52:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:37:25 2008''
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Revision as of 03:52, 4 May 2008

Template:STRUCTURE 2hyw

Human Annexin A2 with Calcium bound


Overview

Annexin A2 and heparin bind to one another with high affinity and in a calcium-dependent manner, an interaction that may play a role in mediating fibrinolysis. In this study, three heparin-derived oligosaccharides of different lengths were co-crystallized with annexin A2 to elucidate the structural basis of the interaction. Crystal structures were obtained at high resolution for uncomplexed annexin A2 and three complexes of heparin oligosaccharides bound to annexin A2. The common heparin-binding site is situated at the convex face of domain IV of annexin A2. At this site, annexin A2 binds up to five sugar residues from the nonreducing end of the oligosaccharide. Unlike most heparin-binding consensus patterns, heparin binding at this site does not rely on arrays of basic residues; instead, main-chain and side-chain nitrogen atoms and two calcium ions play important roles in the binding. Especially significant is a novel calcium-binding site that forms upon heparin binding. Two sugar residues of the heparin derivatives provide oxygen ligands for this calcium ion. Comparison of all four structures shows that heparin binding does not elicit a significant conformational change in annexin A2. Finally, surface plasmon resonance measurements were made for binding interactions between annexin A2 and heparin polysaccharide in solution at pH 7.4 or 5.0. The combined data provide a clear basis for the calcium dependence of heparin binding to annexin A2.

About this Structure

2HYW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystallographic analysis of calcium-dependent heparin binding to annexin A2., Shao C, Zhang F, Kemp MM, Linhardt RJ, Waisman DM, Head JF, Seaton BA, J Biol Chem. 2006 Oct 20;281(42):31689-95. Epub 2006 Aug 1. PMID:16882661 Page seeded by OCA on Sun May 4 06:52:46 2008

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