2c1m: Difference between revisions

Revision as of 05:11, 29 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:2c1m.png

Template:STRUCTURE 2c1m

NUP50:IMPORTIN-ALPHA COMPLEXNUP50:IMPORTIN-ALPHA COMPLEX

Template:ABSTRACT PUBMED 16222336

About this StructureAbout this Structure

2C1M is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Nup50/Npap60 function in nuclear protein import complex disassembly and importin recycling., Matsuura Y, Stewart M, EMBO J. 2005 Nov 2;24(21):3681-9. Epub 2005 Oct 13. PMID:16222336

Page seeded by OCA on Tue Jul 29 05:11:54 2008

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

OCA

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-[[Image:2c1m.gif|left|200px]]
+{{Seed}}
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 {{STRUCTURE_2c1m|  PDB=2c1m  |  SCENE=  }}
-'''NUP50:IMPORTIN-ALPHA COMPLEX'''
+===NUP50:IMPORTIN-ALPHA COMPLEX===
-==Overview==
+<!--
-Nuclear import of proteins containing classical nuclear localization signals (NLS) is mediated by the importin-alpha:beta complex that binds cargo in the cytoplasm and facilitates its passage through nuclear pores, after which nuclear RanGTP dissociates the import complex and the importins are recycled. In vertebrates, import is stimulated by nucleoporin Nup50, which has been proposed to accompany the import complex through nuclear pores. However, we show here that the Nup50 N-terminal domain actively displaces NLSs from importin-alpha, which would be more consistent with Nup50 functioning to coordinate import complex disassembly and importin recycling. The crystal structure of the importin-alpha:Nup50 complex shows that Nup50 binds at two sites on importin-alpha. One site overlaps the secondary NLS-binding site, whereas the second extends along the importin-alpha C-terminus. Mutagenesis indicates that interaction at both sites is required for Nup50 to displace NLSs. The Cse1p:Kap60p:RanGTP complex structure suggests how Nup50 is then displaced on formation of the importin-alpha export complex. These results provide a rationale for understanding the series of interactions that orchestrate the terminal steps of nuclear protein import.
+The line below this paragraph, {{ABSTRACT_PUBMED_16222336}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16222336 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16222336}}
 ==About this Structure==
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 [[Category: Nucleoporin nup50]]
 [[Category: Protein transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 21:06:22 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:11:54 2008''