1zr7

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{{Seed}}
 
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[[Image:1zr7.png|left|200px]]
 
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==Solution structure of the first WW domain of FBP11==
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The line below this paragraph, containing "STRUCTURE_1zr7", creates the "Structure Box" on the page.
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<StructureSection load='1zr7' size='340' side='right'caption='[[1zr7]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1zr7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZR7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZR7 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zr7 OCA], [https://pdbe.org/1zr7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zr7 RCSB], [https://www.ebi.ac.uk/pdbsum/1zr7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zr7 ProSAT]</span></td></tr>
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{{STRUCTURE_1zr7| PDB=1zr7 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PR40A_HUMAN PR40A_HUMAN] Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing.<ref>PMID:21834987</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zr/1zr7_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1zr7 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The Group-II/III WW domains bind Pro-rich sequences, the most frequent protein motif found in eucaryotic genomes. We have proposed that the Group-II and -III WW domains be merged into a larger group because the members of each group have relatively wide specificity and bind to the common ligands [Kato et al., J Biol Chem 2004;279:31833-31841]. We have also proposed that Group-II/III has a common surface patch, the XP2 groove, to bind the ligands. The first WW domain of FBP11/HYPA is one of the Group-II/III WW domains. The solution structure of the 26 residue-long converged region exhibits an antiparallel triple stranded beta-sheet with a small hydrophobic core. The WW domain of FBP11/HYPA has both XP and XP2 grooves on its surface. Ligand titration by 1H-15N HSQC NMR spectra revealed that the WW domain of FBP11/HYPA binds all the peptides with the PL, PP, and PR motifs. The profile patterns of chemical shift perturbation were quite similar among the spectra titrated with all three ligands. In addition, the titration significantly shifts the signals of the residues that compose the XP2 groove. All these findings suggest the functional importance of the XP2 groove and group definition of Group-II/III of the WW domains.
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===Solution structure of the first WW domain of FBP11===
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Solution structure and binding specificity of FBP11/HYPA WW domain as Group-II/III.,Kato Y, Hino Y, Nagata K, Tanokura M Proteins. 2006 Apr 1;63(1):227-34. PMID:16463264<ref>PMID:16463264</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16463264}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1zr7" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16463264 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16463264}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1ZR7 is a 1 chain 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=1ZR7 OCA].
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==Reference==
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<ref group="xtra">PMID:16463264</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Hino, Y.]]
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[[Category: Large Structures]]
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[[Category: Kato, Y.]]
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[[Category: Hino Y]]
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
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[[Category: Kato Y]]
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[[Category: Tanokura, M.]]
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[[Category: Tanokura M]]
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[[Category: Beta sheet]]
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[[Category: National project on protein structural and functional analyse]]
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[[Category: Nppsfa]]
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[[Category: Riken structural genomics/proteomics initiative]]
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[[Category: Rsgi]]
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[[Category: Structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 02:38:37 2009''
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Current revision

Solution structure of the first WW domain of FBP11

PDB ID 1zr7

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