1q1t
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= KPNA2 OR RCH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= KPNA2 OR RCH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ial|1IAL]], [[1ejl|1EJL]], [[1pjm|1PJM]], [[1pjn|1PJN]], [[1ejy|1EJY]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q1t OCA], [http://www.ebi.ac.uk/pdbsum/1q1t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q1t RCSB]</span> | ||
}} | }} | ||
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[[Category: x-ray crystal structure]] | [[Category: x-ray crystal structure]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:07:39 2008'' |
Revision as of 20:07, 30 March 2008
| |||||||
| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | KPNA2 OR RCH1 (Mus musculus) | ||||||
| Related: | 1IAL, 1EJL, 1PJM, 1PJN, 1EJY
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Mouse Importin alpha: non-phosphorylated SV40 CN peptide complex
Overview
The nuclear import of simian-virus-40 large T-antigen (tumour antigen) is enhanced via phosphorylation by the protein kinase CK2 at Ser112 in the vicinity of the NLS (nuclear localization sequence). To determine the structural basis of the effect of the sequences flanking the basic cluster KKKRK, and the effect of phosphorylation on the recognition of the NLS by the nuclear import factor importin-alpha (Impalpha), we co-crystallized non-autoinhibited Impalpha with peptides corresponding to the phosphorylated and non-phosphorylated forms of the NLS, and determined the crystal structures of the complexes. The structures show that the amino acids N-terminally flanking the basic cluster make specific contacts with the receptor that are distinct from the interactions between bipartite NLSs and Impalpha. We confirm the important role of flanking sequences using binding assays. Unexpectedly, the regions of the peptides containing the phosphorylation site do not make specific contacts with the receptor. Binding assays confirm that phosphorylation does not increase the affinity of the T-antigen NLS to Impalpha. We conclude that the sequences flanking the basic clusters in NLSs play a crucial role in nuclear import by modulating the recognition of the NLS by Impalpha, whereas phosphorylation of the T-antigen enhances nuclear import by a mechanism that does not involve a direct interaction of the phosphorylated residue with Impalpha.
About this Structure
1Q1T is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Role of flanking sequences and phosphorylation in the recognition of the simian-virus-40 large T-antigen nuclear localization sequences by importin-alpha., Fontes MR, Teh T, Toth G, John A, Pavo I, Jans DA, Kobe B, Biochem J. 2003 Oct 15;375(Pt 2):339-49. PMID:12852786
Page seeded by OCA on Sun Mar 30 23:07:39 2008
Categories: Mus musculus | Protein complex | Fontes, M R.M. | Jans, D A. | John, A. | Kobe, B. | Pavo, I. | Teh, T. | Toth, G. | Importin alpha/karyopherin alpha | Nuclear localisation sequence (nls) recognition | Phosphorylation | Simian virus (sv40) large tumor-antigen (t-antigen) nl | X-ray crystal structure
