2go5: Difference between revisions
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<StructureSection load='2go5' size='340' side='right' caption='[[2go5]], [[Resolution|resolution]] 7.40Å' scene=''> | <StructureSection load='2go5' size='340' side='right' caption='[[2go5]], [[Resolution|resolution]] 7.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2go5]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Canis_sp. Canis sp.], [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2go5]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Canis_sp. Canis sp.], [http://en.wikipedia.org/wiki/Human Human], [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice] and [http://en.wikipedia.org/wiki/Triticum_sp. Triticum sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GO5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GO5 FirstGlance]. <br> | ||
</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=2go5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2go5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2go5 RCSB], [http://www.ebi.ac.uk/pdbsum/2go5 PDBsum]</span></td></tr> | </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=2go5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2go5 OCA], [http://pdbe.org/2go5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2go5 RCSB], [http://www.ebi.ac.uk/pdbsum/2go5 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2go5" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Canis sp]] | [[Category: Canis sp]] | ||
[[Category: | [[Category: Human]] | ||
[[Category: | [[Category: Lk3 transgenic mice]] | ||
[[Category: Triticum sp]] | [[Category: Triticum sp]] | ||
[[Category: Beckmann, R]] | [[Category: Beckmann, R]] | ||
Revision as of 23:42, 9 September 2015
Structure of signal recognition particle receptor (SR) in complex with signal recognition particle (SRP) and ribosome nascent chain complexStructure of signal recognition particle receptor (SR) in complex with signal recognition particle (SRP) and ribosome nascent chain complex
Structural highlights
Function[SRPRB_MOUSE] Component of the SRP (signal recognition particle) receptor. Ensures, in conjunction with the signal recognition particle, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system. Has GTPase activity. May mediate the membrane association of SRPR. [SRP54_CANFA] Binds to the signal sequence of presecretory protein when they emerge from the ribosomes and transfers them to TRAM (translocating chain-associating membrane protein). [SRPR_HUMAN] Component of the SRP (signal recognition particle) receptor. Ensures, in conjunction with the signal recognition particle, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system. 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 PubMedSignal sequences of secretory and membrane proteins are recognized by the signal recognition particle (SRP) as they emerge from the ribosome. This results in their targeting to the membrane by docking with the SRP receptor, which facilitates transfer of the ribosome to the translocon. Here, we present the 8 angstrom cryo-electron microscopy structure of a "docking complex" consisting of a SRP-bound 80S ribosome and the SRP receptor. Interaction of the SRP receptor with both SRP and the ribosome rearranged the S domain of SRP such that a ribosomal binding site for the translocon, the L23e/L35 site, became exposed, whereas Alu domain-mediated elongation arrest persisted. Signal recognition particle receptor exposes the ribosomal translocon binding site.,Halic M, Gartmann M, Schlenker O, Mielke T, Pool MR, Sinning I, Beckmann R Science. 2006 May 5;312(5774):745-7. PMID:16675701[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also
References
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