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2vgh

From Proteopedia

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[[Image:2vgh.gif|left|200px]]
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{{STRUCTURE_2vgh| PDB=2vgh | SCENE= }}
{{STRUCTURE_2vgh| PDB=2vgh | SCENE= }}
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'''HEPARIN-BINDING DOMAIN FROM VASCULAR ENDOTHELIAL GROWTH FACTOR, NMR, MINIMIZED AVERAGE STRUCTURE'''
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===HEPARIN-BINDING DOMAIN FROM VASCULAR ENDOTHELIAL GROWTH FACTOR, NMR, MINIMIZED AVERAGE STRUCTURE===
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==Overview==
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BACKGROUND: Vascular endothelial growth factor (VEGF) is an endothelial cell-specific mitogen and is a potent angiogenic and vascular permeabilizing factor. VEGF is also an important mediator of pathological angiogenesis associated with cancer, rheumatoid arthritis and proliferative retinopathy. The binding of VEGF to its two known receptors, KDR and Flt-1, is modulated by cell-surface-associated heparin-like glycosaminoglycans and exogenous heparin or heparan sulfate. Heparin binding to VEGF165, the most abundantly expressed isoform of VEGF, has been localized to the carboxy-terminal 55 residues; plasmin cleavage of VEGF165 yields a homodimeric 110-residue amino-terminal receptor-binding domain (VEGF110) and two 55-residue carboxy-terminal heparin-binding fragments. The endothelial cell mitogenic potency of VEGF110 is decreased significantly relative to VEGF165, indicating that the heparin-binding domains are critical for stimulating endothelial cell proliferation. RESULTS: The solution structure of the 55-residue heparin-binding domain of VEGF165 has been solved using data from two-dimensional homonuclear and three-dimensional heteronuclear NMR spectroscopy. The structure has two subdomains, each containing two disulfide bridges and a short two-stranded antiparallel beta sheet; the carboxy-terminal subdomain also contains a short alpha helix. Hydrophobic interactions are limited to sidechains packing against the disulfide bridges. CONCLUSIONS: The heparin-binding domain of VEGF has no significant sequence or structural similarity to any known proteins and thus represents a novel heparin-binding domain. Most of the positively charged amino acid sidechains are localized on one side of the carboxy-terminal subdomain or on an adjacent disordered loop in the amino-terminal subdomain. The observed distribution of surface charges suggests that these residues constitute a heparin interaction site.
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(as it appears on PubMed at http://www.pubmed.gov), where 9634701 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9634701}}
==About this Structure==
==About this Structure==
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2VGH 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=2VGH OCA].
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2VGH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VGH OCA].
==Reference==
==Reference==
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[[Category: Growth factor]]
[[Category: Growth factor]]
[[Category: Heparin-binding]]
[[Category: Heparin-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:45:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:37:17 2008''

Revision as of 02:37, 28 July 2008

Image:2vgh.png

Template:STRUCTURE 2vgh

HEPARIN-BINDING DOMAIN FROM VASCULAR ENDOTHELIAL GROWTH FACTOR, NMR, MINIMIZED AVERAGE STRUCTURE

Template:ABSTRACT PUBMED 9634701

About this Structure

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

Reference

Solution structure of the heparin-binding domain of vascular endothelial growth factor., Fairbrother WJ, Champe MA, Christinger HW, Keyt BA, Starovasnik MA, Structure. 1998 May 15;6(5):637-48. PMID:9634701

Page seeded by OCA on Mon Jul 28 05:37:17 2008

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