1w9c

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(New page: 200px<br /> <applet load="1w9c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w9c, resolution 2.30&Aring;" /> '''PROTEOLYTIC FRAGMEN...)
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caption="1w9c, resolution 2.30&Aring;" />
caption="1w9c, resolution 2.30&Aring;" />
'''PROTEOLYTIC FRAGMENT OF CRM1 SPANNING SIX C-TERMINAL HEAT REPEATS'''<br />
'''PROTEOLYTIC FRAGMENT OF CRM1 SPANNING SIX C-TERMINAL HEAT REPEATS'''<br />
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==About this Structure==
==About this Structure==
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1W9C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W9C OCA].
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1W9C is a [http://en.wikipedia.org/wiki/Single_protein 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==
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[[Category: nuclear protein]]
[[Category: nuclear protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:48:15 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:05:38 2008''

Revision as of 15:05, 15 February 2008


1w9c, resolution 2.30Å

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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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