2z5m: Difference between revisions

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[[Image:2z5m.~~gif~~|left|200px]]

[[Image:2z5m.png|left|200px]]

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~~'''~~Complex of Transportin 1 with TAP NLS, crystal form 2~~'''~~

===Complex of Transportin 1 with TAP NLS, crystal form 2===

~~==Overview==~~

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~~Transportin 1 (Trn1) is a transport receptor that transports substrates from~~ the ~~cytoplasm~~ to the ~~nucleus through nuclear pore complexes by recognizing nuclear localization signals~~ (~~NLSs)~~. ~~Here we describe four crystal structures of human Trn1 in a substrate-free form as well as in the complex with three NLSs (hnRNP D, JKTBP, and TAP, respectively)~~. ~~Our data have revealed that (1~~) ~~Trn1 has two sites for binding NLSs~~, one with high affinity (site A) and one with low affinity (site B), and NLS interaction at site B controls overall binding affinity for Trn1; (2) Trn1 recognizes the NLSs at site A followed by conformational change at site B to interact with the NLSs; and (3) a long flexible loop, characteristic of Trn1, interacts with site B, thereby displacing transport substrate in the ~~nucleus. These studies provide deep understanding of substrate recognition and dissociation by Trn1 in import pathways~~.

The line below this paragraph, {{ABSTRACT_PUBMED_17936704}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17936704 is the PubMed ID number.

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==About this Structure==

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[[Category: Tap]]

[[Category: Transport protein/rna binding protein complex]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 19~~:58:37 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:34:24 2008''

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-[[Image:2z5m.gif|left|200px]]
+{{Seed}}
+[[Image:2z5m.png|left|200px]]
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 {{STRUCTURE_2z5m|  PDB=2z5m  |  SCENE=  }}
-'''Complex of Transportin 1 with TAP NLS, crystal form 2'''
+===Complex of Transportin 1 with TAP NLS, crystal form 2===
-==Overview==
+<!--
-Transportin 1 (Trn1) is a transport receptor that transports substrates from the cytoplasm to the nucleus through nuclear pore complexes by recognizing nuclear localization signals (NLSs). Here we describe four crystal structures of human Trn1 in a substrate-free form as well as in the complex with three NLSs (hnRNP D, JKTBP, and TAP, respectively). Our data have revealed that (1) Trn1 has two sites for binding NLSs, one with high affinity (site A) and one with low affinity (site B), and NLS interaction at site B controls overall binding affinity for Trn1; (2) Trn1 recognizes the NLSs at site A followed by conformational change at site B to interact with the NLSs; and (3) a long flexible loop, characteristic of Trn1, interacts with site B, thereby displacing transport substrate in the nucleus. These studies provide deep understanding of substrate recognition and dissociation by Trn1 in import pathways.
+The line below this paragraph, {{ABSTRACT_PUBMED_17936704}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17936704 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17936704}}
 ==About this Structure==
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 [[Category: Tap]]
 [[Category: Transport protein/rna binding protein complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 19:58:37 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:34:24 2008''