This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1q1t

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1q1t.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1q1t.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1q1t| PDB=1q1t | SCENE= }}
{{STRUCTURE_1q1t| PDB=1q1t | SCENE= }}
-
'''Mouse Importin alpha: non-phosphorylated SV40 CN peptide complex'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12852786}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12852786 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12852786}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Phosphorylation]]
[[Category: Phosphorylation]]
[[Category: X-ray crystal structure]]
[[Category: X-ray crystal structure]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:45:51 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:09:22 2008''

Revision as of 00:09, 28 July 2008

Image:1q1t.png

Template:STRUCTURE 1q1t

Mouse Importin alpha: non-phosphorylated SV40 CN peptide complex

Template:ABSTRACT PUBMED 12852786

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 Mon Jul 28 03:09:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1q1t"
Personal tools