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| - | [[Image:1ejf.gif|left|200px]] | |
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| - | {{Structure
| + | ==CRYSTAL STRUCTURE OF THE HUMAN CO-CHAPERONE P23== |
| - | |PDB= 1ejf |SIZE=350|CAPTION= <scene name='initialview01'>1ejf</scene>, resolution 2.49Å
| + | <StructureSection load='1ejf' size='340' side='right'caption='[[1ejf]], [[Resolution|resolution]] 2.49Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | + | <table><tr><td colspan='2'>[[1ejf]] is a 2 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=1EJF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EJF FirstGlance]. <br> |
| - | |ACTIVITY=
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.49Å</td></tr> |
| - | |GENE=
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | |DOMAIN=
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ejf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ejf OCA], [https://pdbe.org/1ejf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ejf RCSB], [https://www.ebi.ac.uk/pdbsum/1ejf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ejf ProSAT]</span></td></tr> |
| - | |RELATEDENTRY=
| + | </table> |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ejf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ejf OCA], [http://www.ebi.ac.uk/pdbsum/1ejf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ejf RCSB]</span>
| + | == Function == |
| - | }}
| + | [https://www.uniprot.org/uniprot/TEBP_HUMAN TEBP_HUMAN] Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes.<ref>PMID:11274138</ref> <ref>PMID:12077419</ref> <ref>PMID:10922363</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/ej/1ejf_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ejf ConSurf]. |
| | + | <div style="clear:both"></div> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | p23 is a co-chaperone for the heat shock protein, hsp90. This protein binds hsp90 and participates in the folding of a number of cell regulatory proteins, but its activities are still unclear. We have solved a crystal structure of human p23 lacking 35 residues at the COOH terminus. The structure reveals a disulfide-linked dimer with each subunit containing eight beta-strands in a compact antiparallel beta-sandwich fold. In solution, however, p23 is primarily monomeric and the dimer appears to be a minor component. Conserved residues are clustered on one face of the monomer and define a putative surface region and binding pocket for interaction(s) with hsp90 or protein substrates. p23 contains a COOH-terminal tail that is apparently less structured and is unresolved in the crystal structure. This tail is not needed for the binding of p23 to hsp90 or to complexes with the progesterone receptor. However, the tail is necessary for optimum active chaperoning of the progesterone receptor, as well as the passive chaperoning activity of p23 in assays measuring inhibition of heat-induced protein aggregation. |
| | | | |
| - | '''CRYSTAL STRUCTURE OF THE HUMAN CO-CHAPERONE P23'''
| + | Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone.,Weaver AJ, Sullivan WP, Felts SJ, Owen BA, Toft DO J Biol Chem. 2000 Jul 28;275(30):23045-52. PMID:10811660<ref>PMID:10811660</ref> |
| | | | |
| | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | + | </div> |
| | + | <div class="pdbe-citations 1ejf" style="background-color:#fffaf0;"></div> |
| | | | |
| - | ==Overview== | + | ==See Also== |
| - | p23 is a co-chaperone for the heat shock protein, hsp90. This protein binds hsp90 and participates in the folding of a number of cell regulatory proteins, but its activities are still unclear. We have solved a crystal structure of human p23 lacking 35 residues at the COOH terminus. The structure reveals a disulfide-linked dimer with each subunit containing eight beta-strands in a compact antiparallel beta-sandwich fold. In solution, however, p23 is primarily monomeric and the dimer appears to be a minor component. Conserved residues are clustered on one face of the monomer and define a putative surface region and binding pocket for interaction(s) with hsp90 or protein substrates. p23 contains a COOH-terminal tail that is apparently less structured and is unresolved in the crystal structure. This tail is not needed for the binding of p23 to hsp90 or to complexes with the progesterone receptor. However, the tail is necessary for optimum active chaperoning of the progesterone receptor, as well as the passive chaperoning activity of p23 in assays measuring inhibition of heat-induced protein aggregation.
| + | *[[Progesterone receptor|Progesterone receptor]] |
| - | | + | == References == |
| - | ==About this Structure== | + | <references/> |
| - | 1EJF is a [[Single protein]] 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=1EJF OCA].
| + | __TOC__ |
| - | | + | </StructureSection> |
| - | ==Reference==
| + | |
| - | Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone., Weaver AJ, Sullivan WP, Felts SJ, Owen BA, Toft DO, J Biol Chem. 2000 Jul 28;275(30):23045-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10811660 10811660]
| + | |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Single protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Felts, S J.]] | + | [[Category: Felts SJ]] |
| - | [[Category: Owen, B A.L.]] | + | [[Category: Owen BAL]] |
| - | [[Category: Sullivan, W P.]] | + | [[Category: Sullivan WP]] |
| - | [[Category: Toft, D O.]] | + | [[Category: Toft DO]] |
| - | [[Category: Weaver, A J.]] | + | [[Category: Weaver AJ]] |
| - | [[Category: beta-sandwich]]
| + | |
| - | [[Category: chaperone]]
| + | |
| - | [[Category: co-chaperone]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:03:55 2008''
| + | |
| Structural highlights
Function
TEBP_HUMAN Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
p23 is a co-chaperone for the heat shock protein, hsp90. This protein binds hsp90 and participates in the folding of a number of cell regulatory proteins, but its activities are still unclear. We have solved a crystal structure of human p23 lacking 35 residues at the COOH terminus. The structure reveals a disulfide-linked dimer with each subunit containing eight beta-strands in a compact antiparallel beta-sandwich fold. In solution, however, p23 is primarily monomeric and the dimer appears to be a minor component. Conserved residues are clustered on one face of the monomer and define a putative surface region and binding pocket for interaction(s) with hsp90 or protein substrates. p23 contains a COOH-terminal tail that is apparently less structured and is unresolved in the crystal structure. This tail is not needed for the binding of p23 to hsp90 or to complexes with the progesterone receptor. However, the tail is necessary for optimum active chaperoning of the progesterone receptor, as well as the passive chaperoning activity of p23 in assays measuring inhibition of heat-induced protein aggregation.
Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone.,Weaver AJ, Sullivan WP, Felts SJ, Owen BA, Toft DO J Biol Chem. 2000 Jul 28;275(30):23045-52. PMID:10811660[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Forsythe HL, Jarvis JL, Turner JW, Elmore LW, Holt SE. Stable association of hsp90 and p23, but Not hsp70, with active human telomerase. J Biol Chem. 2001 May 11;276(19):15571-4. Epub 2001 Mar 23. PMID:11274138 doi:10.1074/jbc.C100055200
- ↑ Freeman BC, Yamamoto KR. Disassembly of transcriptional regulatory complexes by molecular chaperones. Science. 2002 Jun 21;296(5576):2232-5. PMID:12077419 doi:http://dx.doi.org/10.1126/science.1073051
- ↑ Tanioka T, Nakatani Y, Semmyo N, Murakami M, Kudo I. Molecular identification of cytosolic prostaglandin E2 synthase that is functionally coupled with cyclooxygenase-1 in immediate prostaglandin E2 biosynthesis. J Biol Chem. 2000 Oct 20;275(42):32775-82. PMID:10922363 doi:http://dx.doi.org/10.1074/jbc.M003504200
- ↑ Weaver AJ, Sullivan WP, Felts SJ, Owen BA, Toft DO. Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone. J Biol Chem. 2000 Jul 28;275(30):23045-52. PMID:10811660 doi:10.1074/jbc.M003410200
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