3h0x
From Proteopedia
(Difference between revisions)
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<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=3h0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h0x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3h0x RCSB], [http://www.ebi.ac.uk/pdbsum/3h0x PDBsum], [http://www.topsan.org/Proteins/MCSG/3h0x TOPSAN]</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=3h0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h0x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3h0x RCSB], [http://www.ebi.ac.uk/pdbsum/3h0x PDBsum], [http://www.topsan.org/Proteins/MCSG/3h0x TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/GRP78_YEAST GRP78_YEAST]] Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis.<ref>PMID:16002399</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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]. | </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]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 05:30, 25 December 2014
Crystal structure of peptide-binding domain of Kar2 protein from Saccharomyces cerevisiae
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Categories: Saccharomyces cerevisiae | Bigelow, L | Craig, E A | Gu, M | Joachimiak, A | Structural genomic | Osipiuk, J | Sahi, C | Apc89502 3 | Atp-binding | Bip | Chaperone | Endoplasmic reticulum | Kar2 | Mcsg | Nucleotide-binding | Peptide binding | Phosphoprotein | PSI, Protein structure initiative | Stress response
