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.


1yjm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1yjm.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1yjm.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1yjm| PDB=1yjm | SCENE= }}
{{STRUCTURE_1yjm| PDB=1yjm | SCENE= }}
-
'''Crystal structure of the FHA domain of mouse polynucleotide kinase in complex with an XRCC4-derived phosphopeptide.'''
+
===Crystal structure of the FHA domain of mouse polynucleotide kinase in complex with an XRCC4-derived phosphopeptide.===
-
==Overview==
+
<!--
-
Mammalian polynucleotide kinase (PNK) is a key component of both the base excision repair (BER) and nonhomologous end-joining (NHEJ) DNA repair pathways. PNK acts as a 5'-kinase/3'-phosphatase to create 5'-phosphate/3'-hydroxyl termini, which are a necessary prerequisite for ligation during repair. PNK is recruited to repair complexes through interactions between its N-terminal FHA domain and phosphorylated components of either pathway. Here, we describe the crystal structure of intact mammalian PNK and a structure of the PNK FHA bound to a cognate phosphopeptide. The kinase domain has a broad substrate binding pocket, which preferentially recognizes double-stranded substrates with recessed 5' termini. In contrast, the phosphatase domain efficiently dephosphorylates single-stranded 3'-phospho termini as well as double-stranded substrates. The FHA domain is linked to the kinase/phosphatase catalytic domain by a flexible tether, and it exhibits a mode of target selection based on electrostatic complementarity between the binding surface and the phosphothreonine peptide.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15749016}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15749016 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15749016}}
==About this Structure==
==About this Structure==
Line 39: Line 43:
[[Category: Polynucleotide kinase]]
[[Category: Polynucleotide kinase]]
[[Category: Xrcc4 phosphopeptide]]
[[Category: Xrcc4 phosphopeptide]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:24:13 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:49:25 2008''

Revision as of 03:49, 28 July 2008

Image:1yjm.png

Template:STRUCTURE 1yjm

Crystal structure of the FHA domain of mouse polynucleotide kinase in complex with an XRCC4-derived phosphopeptide.

Template:ABSTRACT PUBMED 15749016

About this Structure

1YJM is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

The molecular architecture of the mammalian DNA repair enzyme, polynucleotide kinase., Bernstein NK, Williams RS, Rakovszky ML, Cui D, Green R, Karimi-Busheri F, Mani RS, Galicia S, Koch CA, Cass CE, Durocher D, Weinfeld M, Glover JN, Mol Cell. 2005 Mar 4;17(5):657-70. PMID:15749016

Page seeded by OCA on Mon Jul 28 06:49:25 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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