1ejy: Difference between revisions

Revision as of 13:28, 21 February 2008

MOUSE IMPORTIN ALPHA-NUCLEOPLASMIN NLS PEPTIDE COMPLEX

OverviewOverview

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 StructureAbout this Structure

1EJY is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 12:28:33 2008

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OCA

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-[[Image:1ejy.gif|left|200px]]<br /><applet load="1ejy" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1ejy, resolution 2.90&Aring;" />
 '''MOUSE IMPORTIN ALPHA-NUCLEOPLASMIN NLS PEPTIDE COMPLEX'''<br />
 ==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.
+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==
-EJY 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EJY OCA].
+EJY 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=1EJY OCA].
 ==Reference==
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 [[Category: Mus musculus]]
 [[Category: Protein complex]]
-[[Category: Fontes, M.R.]]
+[[Category: Fontes, M R.]]
 [[Category: Kobe, B.]]
 [[Category: Teh, T.]]
 [[Category: importin aplpha/karyopherin alpha; nuclear localization sequence (nls) recognition; nucleoplasmin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:04:10 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:28:33 2008''