1jjr
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1jjr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jjr" /> '''The Three-Dimensional Structure of the C-te...)
Next diff →
Revision as of 15:34, 12 November 2007
|
The Three-Dimensional Structure of the C-terminal DNA Binding Domain of Human Ku70
Overview
The proteins Ku70 (69.8 kDa) and Ku80 (82.7 kDa) form a heterodimeric, complex that is an essential component of the nonhomologous end joining, DNA double-strand break repair pathway in mammalian cells. Interaction of, Ku with DNA is central for the functions of Ku. Ku70, which is mainly, responsible for the DNA binding activity of the Ku heterodimer, contains, two DNA-binding domains. We have solved the solution structure of the, Ku80-independent DNA-binding domain of Ku70 encompassing residues 536-609, using nuclear magnetic resonance spectroscopy. Residues 536-560 are highly, flexible and have a random structure but form specific interactions with, DNA. Residues 561-609 of Ku70 form a well defined structure with 3, alpha-helices and also interact with DNA. The three-dimensional structure, indicates that all conserved hydrophobic residues are in the hydrophobic, core and therefore may be important for structural integrity. Most of the, conserved positively charged residues are likely to be critical for DNA, recognition. The C-terminal DNA-binding domain of Ku70 contains a, helix-extended strand-helix motif, which occurs in other nucleic, acid-binding proteins and may represent a common nucleic acid binding, motif.
About this Structure
1JJR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of the C-terminal DNA-binding domain of human Ku70., Zhang Z, Zhu L, Lin D, Chen F, Chen DJ, Chen Y, J Biol Chem. 2001 Oct 12;276(41):38231-6. Epub 2001 Jul 16. PMID:11457852
Page seeded by OCA on Mon Nov 12 17:41:17 2007
