1gy6

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(New page: 200px<br /><applet load="1gy6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gy6, resolution 1.6&Aring;" /> '''NTF2 FROM RAT, AMMONI...)
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[[Image:1gy6.gif|left|200px]]<br /><applet load="1gy6" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1gy6, resolution 1.6&Aring;" />
caption="1gy6, resolution 1.6&Aring;" />
'''NTF2 FROM RAT, AMMONIUM SULPHATE CONDITIONS'''<br />
'''NTF2 FROM RAT, AMMONIUM SULPHATE CONDITIONS'''<br />
==Overview==
==Overview==
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Interactions with nucleoporins containing FxFG-repeat cores are crucial, for the nuclear import of RanGDP mediated by nuclear transport factor 2, (NTF2). We describe here the 1.9 A resolution crystal structure of yeast, NTF2-N77Y bound to a FxFG-nucleoporin core, which provides a basis for, understanding this interaction and its role in nuclear trafficking. The, two identical FxFG binding sites on the dimeric molecule are formed by, residues from each chain of NTF2. Engineered mutants at the interaction, interface reduce the binding of NTF2 to nuclear pores and cause reduced, growth rates and Ran mislocalization when substituted for the wild-type, protein in yeast. Comparison with the crystal structure of FG-nucleoporin, cores bound to importin-beta and TAP/p15 identified a number of common, features of their binding sites. The structure of the binding interfaces, on these transport factors provides a rationale for the specificity of, their interactions with nucleoporins that, combined with their weak, binding constants, facilitates rapid translocation through NPCs during, nuclear trafficking.
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Interactions with nucleoporins containing FxFG-repeat cores are crucial for the nuclear import of RanGDP mediated by nuclear transport factor 2 (NTF2). We describe here the 1.9 A resolution crystal structure of yeast NTF2-N77Y bound to a FxFG-nucleoporin core, which provides a basis for understanding this interaction and its role in nuclear trafficking. The two identical FxFG binding sites on the dimeric molecule are formed by residues from each chain of NTF2. Engineered mutants at the interaction interface reduce the binding of NTF2 to nuclear pores and cause reduced growth rates and Ran mislocalization when substituted for the wild-type protein in yeast. Comparison with the crystal structure of FG-nucleoporin cores bound to importin-beta and TAP/p15 identified a number of common features of their binding sites. The structure of the binding interfaces on these transport factors provides a rationale for the specificity of their interactions with nucleoporins that, combined with their weak binding constants, facilitates rapid translocation through NPCs during nuclear trafficking.
==About this Structure==
==About this Structure==
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1GY6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GY6 OCA].
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1GY6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GY6 OCA].
==Reference==
==Reference==
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[[Category: nuclear transport]]
[[Category: nuclear transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:20:38 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:55:18 2008''

Revision as of 10:55, 21 February 2008


1gy6, resolution 1.6Å

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NTF2 FROM RAT, AMMONIUM SULPHATE CONDITIONS

Overview

Interactions with nucleoporins containing FxFG-repeat cores are crucial for the nuclear import of RanGDP mediated by nuclear transport factor 2 (NTF2). We describe here the 1.9 A resolution crystal structure of yeast NTF2-N77Y bound to a FxFG-nucleoporin core, which provides a basis for understanding this interaction and its role in nuclear trafficking. The two identical FxFG binding sites on the dimeric molecule are formed by residues from each chain of NTF2. Engineered mutants at the interaction interface reduce the binding of NTF2 to nuclear pores and cause reduced growth rates and Ran mislocalization when substituted for the wild-type protein in yeast. Comparison with the crystal structure of FG-nucleoporin cores bound to importin-beta and TAP/p15 identified a number of common features of their binding sites. The structure of the binding interfaces on these transport factors provides a rationale for the specificity of their interactions with nucleoporins that, combined with their weak binding constants, facilitates rapid translocation through NPCs during nuclear trafficking.

About this Structure

1GY6 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Structural basis for the interaction between NTF2 and nucleoporin FxFG repeats., Bayliss R, Leung SW, Baker RP, Quimby BB, Corbett AH, Stewart M, EMBO J. 2002 Jun 17;21(12):2843-53. PMID:12065398

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