This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1ri0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ri0.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ri0.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ri0| PDB=1ri0 | SCENE= }}
{{STRUCTURE_1ri0| PDB=1ri0 | SCENE= }}
-
'''NMR structure of the N-terminal hath domain of human HDGF'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15491618}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15491618 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15491618}}
==About this Structure==
==About this Structure==
-
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].
+
1RI0 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=1RI0 OCA].
==Reference==
==Reference==
Line 30: Line 34:
[[Category: Heparin-binding]]
[[Category: Heparin-binding]]
[[Category: Pwwp domain]]
[[Category: Pwwp domain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:31:20 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:31:06 2008''

Revision as of 13:31, 28 July 2008

Image:1ri0.png

Template:STRUCTURE 1ri0

NMR structure of the N-terminal hath domain of human HDGF

Template:ABSTRACT PUBMED 15491618

About this Structure

1RI0 is a Single protein structure of sequence from Homo sapiens. Full experimental 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 Mon Jul 28 16:31:06 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ri0"
Personal tools