2z5j
From Proteopedia
(New page: 200px<br /> <applet load="2z5j" size="450" color="white" frame="true" align="right" spinBox="true" caption="2z5j, resolution 3.40Å" /> '''Free Transportin 1'...) |
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| - | [[Image:2z5j.gif|left|200px]]<br /> | + | [[Image:2z5j.gif|left|200px]]<br /><applet load="2z5j" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2z5j" size=" | + | |
caption="2z5j, resolution 3.40Å" /> | caption="2z5j, resolution 3.40Å" /> | ||
'''Free Transportin 1'''<br /> | '''Free Transportin 1'''<br /> | ||
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==Overview== | ==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. | 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. | ||
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| - | ==Disease== | ||
| - | Known disease associated with this structure: Deafness, mitochondrial, modifier of OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=610230 610230]] | ||
==About this Structure== | ==About this Structure== | ||
| - | 2Z5J 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:// | + | 2Z5J 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=2Z5J OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:47:30 2008'' |
Revision as of 10:47, 23 January 2008
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Free Transportin 1
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.
About this Structure
2Z5J is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for substrate recognition and dissociation by human transportin 1., Imasaki T, Shimizu T, Hashimoto H, Hidaka Y, Kose S, Imamoto N, Yamada M, Sato M, Mol Cell. 2007 Oct 12;28(1):57-67. PMID:17936704
Page seeded by OCA on Wed Jan 23 12:47:30 2008
