2b8a: Difference between revisions
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< | ==High Resolution Structure of the HDGF PWWP Domain== | ||
<StructureSection load='2b8a' size='340' side='right'caption='[[2b8a]]' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2b8a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B8A FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
-- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2b8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b8a OCA], [https://pdbe.org/2b8a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b8a RCSB], [https://www.ebi.ac.uk/pdbsum/2b8a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b8a ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/HDGF_RAT HDGF_RAT] Heparin-binding protein, with mitogenic activity for fibroblasts. Acts as a transcriptional repressor (By similarity). | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b8/2b8a_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2b8a ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Hepatoma Derived Growth Factor (HDGF) is an endogenous nuclear-targeted mitogen that is linked with human disease. HDGF is a member of the weakly conserved PWWP domain family. This 70-amino acid motif, originally identified from the WHSC1 gene, has been found in more than 60 eukaryotic proteins. In addition to the PWWP domain, many proteins in this class contain known chromatin remodeling domains, suggesting a role for HDGF in chromatin remodeling. We have determined the NMR structure of the HDGF PWWP domain to high resolution using a combination of NOEs, J-couplings, and dipolar couplings. Comparison of this structure to a previously determined structure of the HDGF PWWP domain shows a significant difference in the C-terminal region. Comparison to structures of other PWWP domains shows a high degree of similarity to the PWWP domain structures from Dnmt3b and mHRP. The results of selected and amplified binding assay and NMR titrations with DNA suggest that the HDGF PWWP domain may function as a nonspecific DNA-binding domain. Based on the NMR titrations, we propose a model of the interaction of the PWWP domain with DNA. | |||
High resolution structure of the HDGF PWWP domain: a potential DNA binding domain.,Lukasik SM, Cierpicki T, Borloz M, Grembecka J, Everett A, Bushweller JH Protein Sci. 2006 Feb;15(2):314-23. Epub 2005 Dec 29. PMID:16384999<ref>PMID:16384999</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2b8a" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
< | |||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Borloz | [[Category: Borloz M]] | ||
[[Category: Bushweller | [[Category: Bushweller JH]] | ||
[[Category: Cierpicki | [[Category: Cierpicki T]] | ||
[[Category: Everett | [[Category: Everett A]] | ||
[[Category: Grembecka | [[Category: Grembecka J]] | ||
[[Category: Lukasik | [[Category: Lukasik SM]] | ||
Latest revision as of 12:24, 22 May 2024
High Resolution Structure of the HDGF PWWP DomainHigh Resolution Structure of the HDGF PWWP Domain
Structural highlights
FunctionHDGF_RAT Heparin-binding protein, with mitogenic activity for fibroblasts. Acts as a transcriptional repressor (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHepatoma Derived Growth Factor (HDGF) is an endogenous nuclear-targeted mitogen that is linked with human disease. HDGF is a member of the weakly conserved PWWP domain family. This 70-amino acid motif, originally identified from the WHSC1 gene, has been found in more than 60 eukaryotic proteins. In addition to the PWWP domain, many proteins in this class contain known chromatin remodeling domains, suggesting a role for HDGF in chromatin remodeling. We have determined the NMR structure of the HDGF PWWP domain to high resolution using a combination of NOEs, J-couplings, and dipolar couplings. Comparison of this structure to a previously determined structure of the HDGF PWWP domain shows a significant difference in the C-terminal region. Comparison to structures of other PWWP domains shows a high degree of similarity to the PWWP domain structures from Dnmt3b and mHRP. The results of selected and amplified binding assay and NMR titrations with DNA suggest that the HDGF PWWP domain may function as a nonspecific DNA-binding domain. Based on the NMR titrations, we propose a model of the interaction of the PWWP domain with DNA. High resolution structure of the HDGF PWWP domain: a potential DNA binding domain.,Lukasik SM, Cierpicki T, Borloz M, Grembecka J, Everett A, Bushweller JH Protein Sci. 2006 Feb;15(2):314-23. Epub 2005 Dec 29. PMID:16384999[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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