4etp: Difference between revisions

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 ==C-terminal motor and motor homology domain of Kar3Vik1 fused to a synthetic heterodimeric coiled coil==
-<StructureSection load='4etp' size='340' side='right' caption='[[4etp]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='4etp' size='340' side='right'caption='[[4etp]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4etp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ETP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ETP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4etp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ETP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ETP FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=EBC:N,N-ETHANE-1,2-DIYLBIS(2-IODOACETAMIDE)'>EBC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kar|3kar]], [[2o0a|2o0a]], [[1n6m|1n6m]], [[1u0i|1u0i]], [[1f9t|1f9t]], [[1f9u|1f9u]], [[1f9v|1f9v]], [[1f9w|1f9w]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=EBC:N,N-ETHANE-1,2-DIYLBIS(2-IODOACETAMIDE)'>EBC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KAR3, kar3p, P9659.16, YPR141C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c]), VIK1, Vik1p, YPL253C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</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=4etp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4etp OCA], [https://pdbe.org/4etp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4etp RCSB], [https://www.ebi.ac.uk/pdbsum/4etp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4etp ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4etp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4etp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4etp RCSB], [http://www.ebi.ac.uk/pdbsum/4etp PDBsum]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/KAR3_YEAST KAR3_YEAST] Essential for yeast nuclear fusion during mating. KAR3 is a bifunctional protein having a kinesin-like motor domain joined to a distinct microtubule binding domain. It may mediate microtubule sliding during nuclear fusion and possibly mitosis. May interact with spindle microtubules to produce an inwardly directed force acting upon the poles. KAR3 function antagonizes CIP8 and KIP1 outward force action. KAR3 motor activity is directed toward the microtubule's minus end.<ref>PMID:2138512</ref> <ref>PMID:11729143</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 16: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4etp" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Kinesin 3D Structures|Kinesin 3D Structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Saccharomyces cerevisiae s288c]]
+[[Category: Large Structures]]
-[[Category: Chen, C J]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Cope, J]]
+[[Category: Chen CJ]]
-[[Category: Gilbert, S P]]
+[[Category: Cope J]]
-[[Category: Hoenger, A]]
+[[Category: Gilbert SP]]
-[[Category: Porche, K]]
+[[Category: Hoenger A]]
-[[Category: Rank, K C]]
+[[Category: Porche K]]
-[[Category: Rayment, I]]
+[[Category: Rank KC]]
-[[Category: Internal vik1 crosslink with n]]
+[[Category: Rayment I]]
-[[Category: Karyogamy]]
-[[Category: Kinesin motor homology domain]]
-[[Category: Kinesin motor protein]]
-[[Category: Microtubule]]
-[[Category: Mitosis]]
-[[Category: Motor protein]]
-[[Category: Nucleus]]