1ejl
From Proteopedia
(New page: 200px<br /><applet load="1ejl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ejl, resolution 2.80Å" /> '''MOUSE IMPORTIN ALPHA...) |
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| - | [[Image:1ejl.gif|left|200px]]<br /><applet load="1ejl" size=" | + | [[Image:1ejl.gif|left|200px]]<br /><applet load="1ejl" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ejl, resolution 2.80Å" /> | caption="1ejl, resolution 2.80Å" /> | ||
'''MOUSE IMPORTIN ALPHA-SV40 LARGE T ANTIGEN NLS PEPTIDE COMPLEX'''<br /> | '''MOUSE IMPORTIN ALPHA-SV40 LARGE T ANTIGEN NLS PEPTIDE COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Importin-alpha is the nuclear import receptor that recognizes cargo | + | Importin-alpha is the nuclear import receptor that recognizes cargo proteins which contain classical monopartite and bipartite nuclear localization sequences (NLSs), and facilitates their transport into the nucleus. To determine the structural basis of the recognition of the two classes of NLSs by mammalian importin-alpha, we co-crystallized an N-terminally truncated mouse receptor protein with peptides corresponding to the monopartite NLS from the simian virus 40 (SV40) large T-antigen, and the bipartite NLS from nucleoplasmin. We show that the monopartite SV40 large T-antigen NLS binds to two binding sites on the receptor, similar to what was observed in yeast importin-alpha. The nucleoplasmin NLS-importin-alpha complex shows, for the first time, the mode of binding of bipartite NLSs to the receptor. The two basic clusters in the NLS occupy the two binding sites used by the monopartite NLS, while the sequence linking the two basic clusters is poorly ordered, consistent with its tolerance to mutations. The structures explain the structural basis for binding of diverse NLSs to the sole receptor protein. |
==About this Structure== | ==About this Structure== | ||
| - | 1EJL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1EJL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EJL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Fontes, M | + | [[Category: Fontes, M R.]] |
[[Category: Kobe, B.]] | [[Category: Kobe, B.]] | ||
[[Category: Teh, T.]] | [[Category: Teh, T.]] | ||
[[Category: importin alpha/karyopherin alpha; nuclear localization sequence (nls) recognition; simian virus (sv40) large t-antigen]] | [[Category: importin alpha/karyopherin alpha; nuclear localization sequence (nls) recognition; simian virus (sv40) large t-antigen]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:28:26 2008'' |
Revision as of 10:28, 21 February 2008
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MOUSE IMPORTIN ALPHA-SV40 LARGE T ANTIGEN NLS PEPTIDE COMPLEX
Overview
Importin-alpha is the nuclear import receptor that recognizes cargo proteins which contain classical monopartite and bipartite nuclear localization sequences (NLSs), and facilitates their transport into the nucleus. To determine the structural basis of the recognition of the two classes of NLSs by mammalian importin-alpha, we co-crystallized an N-terminally truncated mouse receptor protein with peptides corresponding to the monopartite NLS from the simian virus 40 (SV40) large T-antigen, and the bipartite NLS from nucleoplasmin. We show that the monopartite SV40 large T-antigen NLS binds to two binding sites on the receptor, similar to what was observed in yeast importin-alpha. The nucleoplasmin NLS-importin-alpha complex shows, for the first time, the mode of binding of bipartite NLSs to the receptor. The two basic clusters in the NLS occupy the two binding sites used by the monopartite NLS, while the sequence linking the two basic clusters is poorly ordered, consistent with its tolerance to mutations. The structures explain the structural basis for binding of diverse NLSs to the sole receptor protein.
About this Structure
1EJL is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-alpha., Fontes MR, Teh T, Kobe B, J Mol Biol. 2000 Apr 14;297(5):1183-94. PMID:10764582
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