1m5n
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1qgk|1QGK]], [[1qgr|1QGR]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m5n OCA], [http://www.ebi.ac.uk/pdbsum/1m5n PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m5n RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
Nuclear import of proteins containing a classical nuclear localization signal (NLS) involves NLS recognition by importin alpha, which associates with importin beta via the IBB domain. Other proteins, including parathyroid hormone-related protein (PTHrP), are imported into the nucleus by direct interaction with importin beta. We solved the crystal structure of a fragment of importin beta-1 (1-485) bound to the nonclassical NLS of PTHrP. The structure reveals a second extended cargo binding site on importin beta distinct from the IBB domain binding site. Using a permeabilized cell import assay we demonstrate that importin beta (1-485) can import PTHrP-coupled cargo in a Ran-dependent manner. We propose that this region contains a prototypical nuclear import receptor domain, which could have evolved into the modern importin beta superfamily. | Nuclear import of proteins containing a classical nuclear localization signal (NLS) involves NLS recognition by importin alpha, which associates with importin beta via the IBB domain. Other proteins, including parathyroid hormone-related protein (PTHrP), are imported into the nucleus by direct interaction with importin beta. We solved the crystal structure of a fragment of importin beta-1 (1-485) bound to the nonclassical NLS of PTHrP. The structure reveals a second extended cargo binding site on importin beta distinct from the IBB domain binding site. Using a permeabilized cell import assay we demonstrate that importin beta (1-485) can import PTHrP-coupled cargo in a Ran-dependent manner. We propose that this region contains a prototypical nuclear import receptor domain, which could have evolved into the modern importin beta superfamily. | ||
- | |||
- | ==Disease== | ||
- | Known disease associated with this structure: Humoral hypercalcemia of malignancy (1) OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=168470 168470]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: heat repeat]] | [[Category: heat repeat]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:11:40 2008'' |
Revision as of 19:11, 30 March 2008
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, resolution 2.90Å | |||||||
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Related: | 1QGK, 1QGR
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of HEAT repeats (1-11) of importin b bound to the non-classical NLS(67-94) of PTHrP
Overview
Nuclear import of proteins containing a classical nuclear localization signal (NLS) involves NLS recognition by importin alpha, which associates with importin beta via the IBB domain. Other proteins, including parathyroid hormone-related protein (PTHrP), are imported into the nucleus by direct interaction with importin beta. We solved the crystal structure of a fragment of importin beta-1 (1-485) bound to the nonclassical NLS of PTHrP. The structure reveals a second extended cargo binding site on importin beta distinct from the IBB domain binding site. Using a permeabilized cell import assay we demonstrate that importin beta (1-485) can import PTHrP-coupled cargo in a Ran-dependent manner. We propose that this region contains a prototypical nuclear import receptor domain, which could have evolved into the modern importin beta superfamily.
About this Structure
1M5N is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Molecular basis for the recognition of a nonclassical nuclear localization signal by importin beta., Cingolani G, Bednenko J, Gillespie MT, Gerace L, Mol Cell. 2002 Dec;10(6):1345-53. PMID:12504010
Page seeded by OCA on Sun Mar 30 22:11:40 2008