1w9c: Difference between revisions
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'''PROTEOLYTIC FRAGMENT OF CRM1 SPANNING SIX C-TERMINAL HEAT REPEATS''' | {{Structure | ||
|PDB= 1w9c |SIZE=350|CAPTION= <scene name='initialview01'>1w9c</scene>, resolution 2.30Å | |||
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'''PROTEOLYTIC FRAGMENT OF CRM1 SPANNING SIX C-TERMINAL HEAT REPEATS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1W9C is a [ | 1W9C is a [[Single protein]] structure of 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=1W9C OCA]. | ||
==Reference== | ==Reference== | ||
Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex., Petosa C, Schoehn G, Askjaer P, Bauer U, Moulin M, Steuerwald U, Soler-Lopez M, Baudin F, Mattaj IW, Muller CW, Mol Cell. 2004 Dec 3;16(5):761-75. PMID:[http:// | Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex., Petosa C, Schoehn G, Askjaer P, Bauer U, Moulin M, Steuerwald U, Soler-Lopez M, Baudin F, Mattaj IW, Muller CW, Mol Cell. 2004 Dec 3;16(5):761-75. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15574331 15574331] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: nuclear protein]] | [[Category: nuclear protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:53:56 2008'' | ||
Revision as of 12:53, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
PROTEOLYTIC FRAGMENT OF CRM1 SPANNING SIX C-TERMINAL HEAT REPEATS
Overview
CRM1/Exportin1 mediates the nuclear export of proteins bearing a leucine-rich nuclear export signal (NES) by forming a cooperative ternary complex with the NES-bearing substrate and the small GTPase Ran. We present a structural model of human CRM1 based on a combination of X-ray crystallography, homology modeling, and electron microscopy. The architecture of CRM1 resembles that of the import receptor transportin1, with 19 HEAT repeats and a large loop implicated in Ran binding. Residues critical for NES recognition are identified adjacent to the cysteine residue targeted by leptomycin B (LMB), a specific CRM1 inhibitor. We present evidence that a conformational change of the Ran binding loop accounts for the cooperativity of Ran- and substrate binding and for the selective enhancement of CRM1-mediated export by the cofactor RanBP3. Our findings indicate that a single architectural and mechanistic framework can explain the divergent effects of RanGTP on substrate binding by many import and export receptors.
About this Structure
1W9C is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex., Petosa C, Schoehn G, Askjaer P, Bauer U, Moulin M, Steuerwald U, Soler-Lopez M, Baudin F, Mattaj IW, Muller CW, Mol Cell. 2004 Dec 3;16(5):761-75. PMID:15574331
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