1e8s: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1e8s]] is a 3 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=1E8S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E8S FirstGlance]. <br> | <table><tr><td colspan='2'>[[1e8s]] is a 3 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=1E8S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E8S FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EU3:EUROPIUM+(III)+ION'>EU3</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EU3:EUROPIUM+(III)+ION'>EU3</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e8o|1e8o]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e8o|1e8o]]</td></tr> | ||
<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=1e8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e8s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e8s RCSB], [http://www.ebi.ac.uk/pdbsum/1e8s PDBsum]</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=1e8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e8s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e8s RCSB], [http://www.ebi.ac.uk/pdbsum/1e8s PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Cusack, S | [[Category: Cusack, S]] | ||
[[Category: Strub, K | [[Category: Strub, K]] | ||
[[Category: Weichenrieder, O | [[Category: Weichenrieder, O]] | ||
[[Category: Wild, K | [[Category: Wild, K]] | ||
[[Category: Alu retroposition]] | [[Category: Alu retroposition]] | ||
[[Category: Alu ribonucleoprotein particle]] | [[Category: Alu ribonucleoprotein particle]] | ||
[[Category: Alu rnp assembly and dimerisation]] | [[Category: Alu rnp assembly and dimerisation]] | ||
[[Category: Translational control]] | [[Category: Translational control]] | ||
Revision as of 21:42, 22 December 2014
Alu domain of the mammalian SRP (potential Alu retroposition intermediate)Alu domain of the mammalian SRP (potential Alu retroposition intermediate)
Structural highlights
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 PubMedThe Alu domain of the mammalian signal recognition particle (SRP) comprises the heterodimer of proteins SRP9 and SRP14 bound to the 5' and 3' terminal sequences of SRP RNA. It retards the ribosomal elongation of signal-peptide-containing proteins before their engagement with the translocation machinery in the endoplasmic reticulum. Here we report two crystal structures of the heterodimer SRP9/14 bound either to the 5' domain or to a construct containing both 5' and 3' domains. We present a model of the complete Alu domain that is consistent with extensive biochemical data. SRP9/14 binds strongly to the conserved core of the 5' domain, which forms a U-turn connecting two helical stacks. Reversible docking of the more weakly bound 3' domain might be functionally important in the mechanism of translational regulation. The Alu domain structure is probably conserved in other cytoplasmic ribonucleoprotein particles and retroposition intermediates containing SRP9/14-bound RNAs transcribed from Alu repeats or related elements in genomic DNA. Structure and assembly of the Alu domain of the mammalian signal recognition particle.,Weichenrieder O, Wild K, Strub K, Cusack S Nature. 2000 Nov 9;408(6809):167-73. PMID:11089964[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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