2hgf
From Proteopedia
(New page: 200px<br /> <applet load="2hgf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hgf" /> '''HAIRPIN LOOP CONTAINING DOMAIN OF HEPATOCYT...) |
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'''HAIRPIN LOOP CONTAINING DOMAIN OF HEPATOCYTE GROWTH FACTOR, NMR, MINIMIZED AVERAGE STRUCTURE'''<br /> | '''HAIRPIN LOOP CONTAINING DOMAIN OF HEPATOCYTE GROWTH FACTOR, NMR, MINIMIZED AVERAGE STRUCTURE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2HGF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2HGF is a [http://en.wikipedia.org/wiki/Single_protein 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=2HGF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: scatter factor]] | [[Category: scatter factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:31:57 2008'' |
Revision as of 15:31, 15 February 2008
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HAIRPIN LOOP CONTAINING DOMAIN OF HEPATOCYTE GROWTH FACTOR, NMR, MINIMIZED AVERAGE STRUCTURE
Contents |
Overview
BACKGROUND: Hepatocyte growth factor (HGF) is a multipotent growth factor, that transduces a wide range of biological signals, including mitogenesis, motogenesis, and morphogenesis. The N-terminal (N) domain of HGF, containing a hairpin-loop region, is important for receptor binding and, the potent biological activities of HGF. The N domain is also the primary, binding site for heparin or heparan sulfate, which enhances, receptor/ligand oligomerization and modulates receptor-dependent, mitogenesis. The rational design of artificial modulators of HGF signaling, requires a detailed understanding of the structures of HGF and its, receptor, as well as the role of heparin proteoglycan; this study, represents the first step towards that goal. RESULTS: We report here a, high-resolution structure of the N domain of HGF. This first structure of, HGF reveals a novel folding topology with a distinct pattern of charge, distribution and indicates a possible heparin-binding site. CONCLUSIONS:, The hairpin-loop region of the N domain plays a major role in stabilizing, the structure and contributes to a putative heparin-binding site, which, explains why it is required for biological functions. These results, suggest several basic and/or polar residues that may be important for use, in further mutational studies of heparin binding.
Disease
Known diseases associated with this structure: Fibromatosis, gingival OMIM:[182530], Noonan syndrome 4 OMIM:[182530]
About this Structure
2HGF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The solution structure of the N-terminal domain of hepatocyte growth factor reveals a potential heparin-binding site., Zhou H, Mazzulla MJ, Kaufman JD, Stahl SJ, Wingfield PT, Rubin JS, Bottaro DP, Byrd RA, Structure. 1998 Jan 15;6(1):109-16. PMID:9493272
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