View source for 1ipg


==SOLUTION STRUCTURE OF THE PB1 DOMAIN OF BEM1P==
<StructureSection load='1ipg' size='340' side='right'caption='[[1ipg]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ipg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IPG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IPG 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=1ipg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ipg OCA], [https://pdbe.org/1ipg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ipg RCSB], [https://www.ebi.ac.uk/pdbsum/1ipg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ipg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BEM1_YEAST BEM1_YEAST] Necessary for cell polarization during vegetative growth. May link the cytoskeleton to morphogenic determinants on the cell surface.<ref>PMID:17460121</ref> 
== 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/ip/1ipg_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=1ipg ConSurf].
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== Publication Abstract from PubMed ==
PB1 domains are novel protein modules capable of binding to target proteins that contain PC motifs. We report here the NMR structure and ligand-binding site of the PB1 domain of the cell polarity establishment protein, Bem1p. In addition, we identify the topology of the PC motif-containing region of Cdc24p by NMR, another cell polarity establishment protein that interacts with Bem1p. The PC motif-containing region is a structural domain offering a scaffold to the PC motif. The chemical shift perturbation experiment and the mutagenesis study show that the PC motif is a major structural element that binds to the PB1 domain. A structural database search reveals close similarity between the Bem1p PB1 domain and the c-Raf1 Ras-binding domain. However, these domains are functionally distinct from each other.

Structure and ligand recognition of the PB1 domain: a novel protein module binding to the PC motif.,Terasawa H, Noda Y, Ito T, Hatanaka H, Ichikawa S, Ogura K, Sumimoto H, Inagaki F EMBO J. 2001 Aug 1;20(15):3947-56. PMID:11483498<ref>PMID:11483498</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1ipg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Hatanaka H]]
[[Category: Ichikawa S]]
[[Category: Inagaki F]]
[[Category: Ito T]]
[[Category: Noda Y]]
[[Category: Ogura K]]
[[Category: Sumimoto H]]
[[Category: Terasawa H]]