2z5m: Difference between revisions
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New page: left|200px<br /> <applet load="2z5m" size="450" color="white" frame="true" align="right" spinBox="true" caption="2z5m, resolution 3.00Å" /> '''Complex of Transpor... |
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[[Image:2z5m.gif|left|200px]]<br /> | [[Image:2z5m.gif|left|200px]]<br /><applet load="2z5m" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="2z5m" size=" | |||
caption="2z5m, resolution 3.00Å" /> | caption="2z5m, resolution 3.00Å" /> | ||
'''Complex of Transportin 1 with TAP NLS, crystal form 2'''<br /> | '''Complex of Transportin 1 with TAP NLS, crystal form 2'''<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. | ||
==About this Structure== | ==About this Structure== | ||
2Z5M is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 2Z5M is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=2Z5M OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transport protein/rna binding protein complex]] | [[Category: transport protein/rna binding protein complex]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:47:34 2008'' | ||
