1q1o: Difference between revisions

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-{{Seed}}
-[[Image:1q1o.png|left|200px]]
-<!--
+==Solution Structure of the PB1 Domain of Cdc24p (Long Form)==
-The line below this paragraph, containing "STRUCTURE_1q1o", creates the "Structure Box" on the page.
+<StructureSection load='1q1o' size='340' side='right'caption='[[1q1o]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1q1o]] 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=1Q1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q1O FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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=1q1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q1o OCA], [https://pdbe.org/1q1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q1o RCSB], [https://www.ebi.ac.uk/pdbsum/1q1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q1o ProSAT]</span></td></tr>
-{{STRUCTURE_1q1o|  PDB=1q1o  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CDC24_YEAST CDC24_YEAST] Promotes the exchange of CDC42-bound GDP by GTP. Controls the polarity of calmodulin, and the calcium regulatory process of bud emergence. CDC24 may be involved in the initial selection and organization of the budding site.
+== 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/q1/1q1o_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=1q1o ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The PC motif is evolutionarily conserved together with the PB1 domain, a binding partner of the PC motif-containing protein. For interaction with the PB1 domain, the PC motif-containing region (PCCR) comprising the PC motif and its flanking regions is required. Because the PB1 domain and the PCCR are novel binding modules found in a variety of signaling proteins, their structural and functional characterization is crucial. Bem1p and Cdc24p interact through the PB1-PCCR interaction and regulate cell polarization in budding yeast. Here, we determined a tertiary structure of the PCCR of Cdc24p by NMR. The tertiary structure of the PCCR is similar to that of the PB1 domain of Bem1p, which is classified into a ubiquitin fold. The PC motif portion takes a compact betabetaalpha-fold, presented on the ubiquitin scaffold. Mutational studies indicate that the PB1-PCCR interaction is mainly electrostatic. Based on the structural information, we group the PB1 domains and the PCCRs into a novel family, named the PB1 family. Thus, the PB1 family proteins form a specific dimer with each other.
-===Solution Structure of the PB1 Domain of Cdc24p (Long Form)===
+The PB1 domain and the PC motif-containing region are structurally similar protein binding modules.,Yoshinaga S, Kohjima M, Ogura K, Yokochi M, Takeya R, Ito T, Sumimoto H, Inagaki F EMBO J. 2003 Oct 1;22(19):4888-97. PMID:14517229<ref>PMID:14517229</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_14517229}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1q1o" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 14517229 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_14517229}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-Q1O is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q1O OCA].
-==Reference==
-<ref group="xtra">PMID:14517229</ref><references group="xtra"/>
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Inagaki, F.]]
+[[Category: Inagaki F]]
-[[Category: Ito, T.]]
+[[Category: Ito T]]
-[[Category: Kohjima, M.]]
+[[Category: Kohjima M]]
-[[Category: Ogura, K.]]
+[[Category: Ogura K]]
-[[Category: Sumimoto, H.]]
+[[Category: Sumimoto H]]
-[[Category: Takeya, R.]]
+[[Category: Takeya R]]
-[[Category: Yokochi, M.]]
+[[Category: Yokochi M]]
-[[Category: Yoshinaga, S.]]
+[[Category: Yoshinaga S]]
-[[Category: Cell polarity]]
-[[Category: Opca motif]]
-[[Category: Pb1 domain]]
-[[Category: Pc motif]]
-[[Category: Pccr]]
-[[Category: Protein-protein interaction]]
-[[Category: Yeast]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 06:35:59 2009''