2nlu: Difference between revisions

Revision as of 19:38, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2nlu.png

Template:STRUCTURE 2nlu

Domain-Swapped Dimer of the PWWP Module of Human Hepatoma-derived Growth FactorDomain-Swapped Dimer of the PWWP Module of Human Hepatoma-derived Growth Factor

Template:ABSTRACT PUBMED 17270212

About this StructureAbout this Structure

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

ReferenceReference

PWWP module of human hepatoma-derived growth factor forms a domain-swapped dimer with much higher affinity for heparin., Sue SC, Lee WT, Tien SC, Lee SC, Yu JG, Wu WJ, Wu WG, Huang TH, J Mol Biol. 2007 Mar 23;367(2):456-72. Epub 2007 Jan 9. PMID:17270212

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-'''Domain-Swapped Dimer of the PWWP Module of Human Hepatoma-derived Growth Factor'''
+===Domain-Swapped Dimer of the PWWP Module of Human Hepatoma-derived Growth Factor===
-==Overview==
+<!--
-Hepatoma-derived growth factor (hHDGF)-related proteins (HRPs) comprise a new growth factor family sharing a highly conserved and ordered N-terminal PWWP module (residues 1-100, previously referred to as a HATH domain) and a variable disordered C-terminal domain. We have shown that the PWWP module is responsible for heparin binding and have solved its structure in solution. Here, we show that under physiological conditions, both the PWWP module and hHDGF can form dimers. Surface plasmon resonance (SPR) studies revealed that the PWWP dimer binds to heparin with affinity that is two orders of magnitude higher (K(d)=13 nM) than that of the monomeric PWWP module (K(d)=1.2 microM). The monomer-dimer equilibrium properties and NMR structural data together suggest that the PWWP dimer is formed through a domain-swapping mechanism. The domain-swapped PWWP dimer structures were calculated on the basis of the NMR data. The results show that the two PWWP protomers exchange their N-terminal hairpin to form a domain-swapped dimer. The two monomers in a dimer are linked by the long flexible L2 loops, a feature supported by NMR relaxation data for the monomer and dimer. The enhanced heparin-binding affinity of the dimer can be rationalized in the framework of the dimer structure.
+The line below this paragraph, {{ABSTRACT_PUBMED_17270212}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17270212 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17270212}}
 ==About this Structure==
-NLU 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=2NLU OCA].
+NLU 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=2NLU OCA].
 ==Reference==
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 [[Category: Hrp]]
 [[Category: Pwwp]]
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