View source for 1n27


==Solution structure of the PWWP domain of mouse Hepatoma-derived growth factor, related protein 3==
<StructureSection load='1n27' size='340' side='right'caption='[[1n27]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1n27]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N27 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N27 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=1n27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n27 OCA], [https://pdbe.org/1n27 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n27 RCSB], [https://www.ebi.ac.uk/pdbsum/1n27 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n27 ProSAT], [https://www.topsan.org/Proteins/RSGI/1n27 TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HDGR3_MOUSE HDGR3_MOUSE] Enhances DNA synthesis and may play a role in cell proliferation (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/n2/1n27_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=1n27 ConSurf].
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== Publication Abstract from PubMed ==
Among the many PWWP-containing proteins, the largest group of homologous proteins is related to hepatoma-derived growth factor (HDGF). Within a well-conserved region at the extreme N-terminus, HDGF and five HDGF-related proteins (HRPs) always have a PWWP domain, which is a module found in many chromatin-associated proteins. In this study, we determined the solution structure of the PWWP domain of HDGF-related protein-3 (HRP-3) by NMR spectroscopy. The structure consists of a five-stranded beta-barrel with a PWWP-specific long loop connecting beta2 and beta3 (PR-loop), followed by a helical region including two alpha-helices. Its structure was found to have a characteristic solvent-exposed hydrophobic cavity, which is composed of an abundance of aromatic residues in the beta1/beta2 loop (beta-beta arch) and the beta3/beta4 loop. A similar ligand binding cavity occurs at the corresponding position in the Tudor, chromo, and MBT domains, which have structural and probable evolutionary relationships with PWWP domains. These findings suggest that the PWWP domains of the HDGF family bind to some component of chromatin via the cavity.

Solution structure of the PWWP domain of the hepatoma-derived growth factor family.,Nameki N, Tochio N, Koshiba S, Inoue M, Yabuki T, Aoki M, Seki E, Matsuda T, Fujikura Y, Saito M, Ikari M, Watanabe M, Terada T, Shirouzu M, Yoshida M, Hirota H, Tanaka A, Hayashizaki Y, Guntert P, Kigawa T, Yokoyama S Protein Sci. 2005 Mar;14(3):756-64. Epub 2005 Feb 2. PMID:15689505<ref>PMID:15689505</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Inoue M]]
[[Category: Kigawa T]]
[[Category: Kobayashi N]]
[[Category: Koshiba S]]
[[Category: Nameki N]]
[[Category: Tochio N]]
[[Category: Yokoyama S]]