1ri0
From Proteopedia
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| - | [[Image:1ri0.gif|left|200px]] | + | [[Image:1ri0.gif|left|200px]] |
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| - | '''NMR structure of the N-terminal hath domain of human HDGF''' | + | {{Structure |
| + | |PDB= 1ri0 |SIZE=350|CAPTION= <scene name='initialview01'>1ri0</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= HDGF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''NMR structure of the N-terminal hath domain of human HDGF''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RI0 is a [ | + | 1RI0 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=1RI0 OCA]. |
==Reference== | ==Reference== | ||
| - | Solution structure and heparin interaction of human hepatoma-derived growth factor., Sue SC, Chen JY, Lee SC, Wu WG, Huang TH, J Mol Biol. 2004 Nov 5;343(5):1365-77. PMID:[http:// | + | Solution structure and heparin interaction of human hepatoma-derived growth factor., Sue SC, Chen JY, Lee SC, Wu WG, Huang TH, J Mol Biol. 2004 Nov 5;343(5):1365-77. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15491618 15491618] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: pwwp domain]] | [[Category: pwwp domain]] | ||
| - | ''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 13:51:54 2008'' |
Revision as of 11:51, 20 March 2008
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| Gene: | HDGF (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR structure of the N-terminal hath domain of human HDGF
Overview
Hepatoma-derived growth factor (HDGF)-related proteins (HRPs) comprise a new protein family that has been implicated in nephrogenesis, tumorigenesis, vascular development, cell proliferation, and transcriptional activation. All HRPs share a conserved N-terminal homologous to the amino terminus of HDGF (HATH) domain, but vary significantly in the C-terminal region. Here, we show that in solution the N and C termini of human HDGF form two structurally independent domains. The 100 amino acid residue N-terminal HATH domain is well-structured while the 140 amino acid residue C-terminal domain is disordered. We determined the solution structure of the HATH domain by NMR. The core structure of the HATH domain is a five-stranded beta-barrel followed by two alpha-helices, similar to those of PWWP domains of known structures. Surface plasmon resonance results showed that the HATH domain is primarily responsible for heparin binding. On the basis of the chemical shift perturbation induced by binding of heparin-derived hexasaccharide, we identified a prominent, highly positively charged region as the putative heparin-binding site. Sequence comparison and structure prediction suggest that all HRPs are likely to adapt a similar modular structure.
About this Structure
1RI0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure and heparin interaction of human hepatoma-derived growth factor., Sue SC, Chen JY, Lee SC, Wu WG, Huang TH, J Mol Biol. 2004 Nov 5;343(5):1365-77. PMID:15491618
Page seeded by OCA on Thu Mar 20 13:51:54 2008
