2w0g

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{{Seed}}
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==HSP90 CO-CHAPERONE CDC37==
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[[Image:2w0g.png|left|200px]]
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<StructureSection load='2w0g' size='340' side='right' caption='[[2w0g]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2w0g]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2W0G FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1us7|1us7]]</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2w0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2w0g RCSB], [http://www.ebi.ac.uk/pdbsum/2w0g PDBsum]</span></td></tr>
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<table>
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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/w0/2w0g_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/chain_selection.php?pdb_ID=2ata 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 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.
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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>
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The line below this paragraph, containing "STRUCTURE_2w0g", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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-->
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{{STRUCTURE_2w0g| PDB=2w0g | SCENE= }}
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===HSP90 CO-CHAPERONE CDC37===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<!--
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_19073599}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 19073599 is the PubMed ID number.
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</StructureSection>
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-->
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{{ABSTRACT_PUBMED_19073599}}
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==About this Structure==
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2W0G 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].
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==Reference==
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<ref group="xtra">PMID:19073599</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Jonker, H R.A.]]
[[Category: Jonker, H R.A.]]
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[[Category: Chaperone]]
[[Category: Chaperone]]
[[Category: Chaperone co- chaperone regulation]]
[[Category: Chaperone co- chaperone regulation]]
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[[Category: Cytoplasm]]
 
[[Category: Heat shock]]
[[Category: Heat shock]]
[[Category: Nucleotide-binding]]
[[Category: Nucleotide-binding]]
[[Category: Phosphoprotein]]
[[Category: Phosphoprotein]]
[[Category: Phosphorylation]]
[[Category: Phosphorylation]]
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[[Category: Polymorphism]]
 
[[Category: Stress response]]
[[Category: Stress response]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 15 08:45:42 2009''
 

Revision as of 10:40, 28 May 2014

HSP90 CO-CHAPERONE CDC37

2w0g, resolution 1.88Å

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