2qna: Difference between revisions

Revision as of 06:05, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2qna.png

Template:STRUCTURE 2qna

Crystal structure of human Importin-beta (127-876) in complex with the IBB-domain of Snurportin1 (1-65)Crystal structure of human Importin-beta (127-876) in complex with the IBB-domain of Snurportin1 (1-65)

Template:ABSTRACT PUBMED 18028944

About this StructureAbout this Structure

2QNA is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for RanGTP independent entry of spliceosomal U snRNPs into the nucleus., Wohlwend D, Strasser A, Dickmanns A, Ficner R, J Mol Biol. 2007 Dec 7;374(4):1129-38. Epub 2007 Sep 29. PMID:18028944

Page seeded by OCA on Mon Jul 28 06:05:41 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2qna.jpg|left|200px]]
+{{Seed}}
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 {{STRUCTURE_2qna|  PDB=2qna  |  SCENE=  }}
-'''Crystal structure of human Importin-beta (127-876) in complex with the IBB-domain of Snurportin1 (1-65)'''
+===Crystal structure of human Importin-beta (127-876) in complex with the IBB-domain of Snurportin1 (1-65)===
-==Overview==
+<!--
-The nuclear import of assembled spliceosomal subunits, the uridine-rich small nuclear ribonucleoprotein particles (U snRNPs), is mediated by a nuclear import receptor adaptor couple of importin beta (Imp beta) and snurportin1 (SPN1). In contrast to any other characterized active nuclear import, the Imp beta/SPN1/U snRNP complex does not require RanGTP for the terminal release from the nuclear basket of the nuclear pore complex (NPC). The crystal structure of Imp beta (127-876) in complex with the Imp beta-binding (IBB) domain of SPN1 (1-65) at 2.8-A resolution reveals that Imp beta adopts an open conformation, which is unique for a functional Imp beta/cargo complex, and rather surprisingly, it resembles the conformation of the Imp beta/RanGTP complex. As binding of RanGTP to Imp beta usually triggers the release of import complexes from the NPC, we propose that by already mimicking a conformation similar to Imp beta/RanGTP the independent dissociation of Imp beta/SPN1 from the nuclear basket is energetically aided.
+The line below this paragraph, {{ABSTRACT_PUBMED_18028944}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18028944 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18028944}}
 ==About this Structure==
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 [[Category: Rna-binding]]
 [[Category: Transport protein]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:05:41 2008''