2w0g: Difference between revisions

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-{{Seed}}
-[[Image:2w0g.png|left|200px]]
-<!--
+==HSP90 CO-CHAPERONE CDC37==
-The line below this paragraph, containing "STRUCTURE_2w0g", creates the "Structure Box" on the page.
+<StructureSection load='2w0g' size='340' side='right'caption='[[2w0g]], [[Resolution|resolution]] 1.88&Aring;' 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'>[[2w0g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W0G 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">X-ray diffraction, [[Resolution|Resolution]] 1.88&#8491;</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=2w0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w0g OCA], [https://pdbe.org/2w0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w0g RCSB], [https://www.ebi.ac.uk/pdbsum/2w0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w0g ProSAT]</span></td></tr>
-{{STRUCTURE_2w0g|  PDB=2w0g  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CDC37_HUMAN CDC37_HUMAN] Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity.<ref>PMID:8666233</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/w0/2w0g_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=2w0g ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The cell division cycle protein 37 (Cdc37) and the 90-kDa heat shock protein (Hsp90) are molecular chaperones, which are crucial elements in the protein signaling pathway. The largest class of client proteins for Cdc37 and Hsp90 are protein kinases. The catalytic domains of these kinases are stabilized by Cdc37, and their proper folding and functioning is dependent on Hsp90. Here, we present the x-ray crystal structure of the 16-kDa middle domain of human Cdc37 at 1.88 angstroms resolution and the structure of this domain in complex with the 23-kDa N-terminal domain of human Hsp90 based on heteronuclear solution state NMR data and docking. Our results demonstrate that the middle domain of Cdc37 exists as a monomer. NMR and mutagenesis experiments reveal Leu-205 in Cdc37 as a key residue enabling complex formation. These findings can be very useful in the development of small molecule inhibitors against cancer.
-===HSP90 CO-CHAPERONE CDC37===
+The human Cdc37.Hsp90 complex studied by heteronuclear NMR spectroscopy.,Sreeramulu S, Jonker HR, Langer T, Richter C, Lancaster CR, Schwalbe H J Biol Chem. 2009 Feb 6;284(6):3885-96. Epub 2008 Dec 10. PMID:19073599<ref>PMID:19073599</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_19073599}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2w0g" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 19073599 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_19073599}}
+__TOC__
+</StructureSection>
-==About this Structure==
-W0G is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W0G OCA].
-==Reference==
-The human CDC37.HSP90 complex studied by heteronuclear NMR spectroscopy., Sreeramulu S, Jonker HR, Langer T, Richter C, Lancaster CR, Schwalbe H, J Biol Chem. 2008 Dec 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/19073599 19073599]
 [[Category: Homo sapiens]]
-[[Category: Jonker, H R.A.]]
+[[Category: Large Structures]]
-[[Category: Lancaster, C R.D.]]
+[[Category: Jonker HRA]]
-[[Category: Schwalbe, H.]]
+[[Category: Lancaster CRD]]
-[[Category: Sreeramulu, S.]]
+[[Category: Schwalbe H]]
-[[Category: Atp-binding]]
+[[Category: Sreeramulu S]]
-[[Category: Chaperone]]
-[[Category: Chaperone co- chaperone regulation]]
-[[Category: Cytoplasm]]
-[[Category: Heat shock]]
-[[Category: Nucleotide-binding]]
-[[Category: Phosphoprotein]]
-[[Category: Phosphorylation]]
-[[Category: Polymorphism]]
-[[Category: Stress response]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 31 09:04:18 2008''