1pjm
From Proteopedia
(New page: 200px<br /> <applet load="1pjm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pjm, resolution 2.50Å" /> '''Mouse Importin alph...) |
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| - | [[Image:1pjm.gif|left|200px]]<br /> | + | [[Image:1pjm.gif|left|200px]]<br /><applet load="1pjm" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1pjm" size=" | + | |
caption="1pjm, resolution 2.50Å" /> | caption="1pjm, resolution 2.50Å" /> | ||
'''Mouse Importin alpha-bipartite NLS from human retinoblastoma protein Complex'''<br /> | '''Mouse Importin alpha-bipartite NLS from human retinoblastoma protein 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 carrying conventional basic monopartite and bipartite nuclear localization sequences (NLSs) and facilitates their transport into the nucleus. Bipartite NLSs contain two clusters of basic residues, connected by linkers of variable lengths. To determine the structural basis of the recognition of diverse bipartite NLSs by mammalian importin-alpha, we co-crystallized a non-autoinhibited mouse receptor protein with peptides corresponding to the NLSs from human retinoblastoma protein and Xenopus laevis phosphoprotein N1N2, containing diverse sequences and lengths of the linker. We show that the basic clusters interact analogously in both NLSs, but the linker sequences adopt different conformations, whereas both make specific contacts with the receptor. The available data allow us to draw general conclusions about the specificity of NLS binding by importin-alpha and facilitate an improved definition of the consensus sequence of a conventional basic/bipartite NLS (KRX10-12KRRK) that can be used to identify novel nuclear proteins. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PJM 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:// | + | 1PJM 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=1PJM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Brinkworth, R | + | [[Category: Brinkworth, R I.]] |
| - | [[Category: Fontes, M | + | [[Category: Fontes, M R.M.]] |
[[Category: Jans, D.]] | [[Category: Jans, D.]] | ||
[[Category: Kobe, B.]] | [[Category: Kobe, B.]] | ||
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[[Category: nuclear localization sequence (nls) recognition]] | [[Category: nuclear localization sequence (nls) recognition]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:29:27 2008'' |
Revision as of 12:29, 21 February 2008
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Mouse Importin alpha-bipartite NLS from human retinoblastoma protein Complex
Contents |
Overview
Importin-alpha is the nuclear import receptor that recognizes cargo proteins carrying conventional basic monopartite and bipartite nuclear localization sequences (NLSs) and facilitates their transport into the nucleus. Bipartite NLSs contain two clusters of basic residues, connected by linkers of variable lengths. To determine the structural basis of the recognition of diverse bipartite NLSs by mammalian importin-alpha, we co-crystallized a non-autoinhibited mouse receptor protein with peptides corresponding to the NLSs from human retinoblastoma protein and Xenopus laevis phosphoprotein N1N2, containing diverse sequences and lengths of the linker. We show that the basic clusters interact analogously in both NLSs, but the linker sequences adopt different conformations, whereas both make specific contacts with the receptor. The available data allow us to draw general conclusions about the specificity of NLS binding by importin-alpha and facilitate an improved definition of the consensus sequence of a conventional basic/bipartite NLS (KRX10-12KRRK) that can be used to identify novel nuclear proteins.
Disease
Known diseases associated with this structure: Bladder cancer OMIM:[180200], Osteosarcoma OMIM:[180200], Pinealoma with bilateral retinoblastoma OMIM:[180200], Retinoblastoma OMIM:[180200]
About this Structure
1PJM is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural basis for the specificity of bipartite nuclear localization sequence binding by importin-alpha., Fontes MR, Teh T, Jans D, Brinkworth RI, Kobe B, J Biol Chem. 2003 Jul 25;278(30):27981-7. Epub 2003 Apr 14. PMID:12695505
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