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1q2z

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{{STRUCTURE_1q2z| PDB=1q2z | SCENE= }}
{{STRUCTURE_1q2z| PDB=1q2z | SCENE= }}
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'''The 3D solution structure of the C-terminal region of Ku86'''
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===The 3D solution structure of the C-terminal region of Ku86===
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==Overview==
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In eukaryotes the non-homologous end-joining repair of double strand breaks in DNA is executed by a series of proteins that bring about the synapsis, preparation and ligation of the broken DNA ends. The mechanism of this process appears to be initiated by the obligate heterodimer (Ku70/Ku86) protein complex Ku that has affinity for DNA ends. Ku then recruits the DNA-dependent protein kinase catalytic subunit (DNA-PKcs). The three-dimensional structures of the major part of the Ku heterodimer, representing the DNA-binding core, both free and bound to DNA are known from X-ray crystallography. However, these structures lack a region of ca 190 residues from the C-terminal region (CTR) of the Ku86 subunit (also known as Lupus Ku autoantigen p86, Ku80, or XRCC5) that includes the extreme C-terminal tail that is reported to be sufficient for DNA-PKcs-binding. We have examined the structural characteristics of the Ku86CTR protein expressed in bacteria. By deletion mutagenesis and heteronuclear NMR spectroscopy we localised a globular domain consisting of residues 592-709. Constructs comprising additional residues either to the N-terminal side (residues 543-709), or the C-terminal side (residues 592-732), which includes the putative DNA-PKcs-binding motif, yielded NMR spectra consistent with these extra regions lacking ordered structure. The three-dimensional solution structure of the core globular domain of the C-terminal region of Ku86 (Ku86CTR(592-709)) has been determined using heteronuclear NMR spectroscopy and dynamical simulated annealing using structural restraints from nuclear Overhauser effect spectroscopy, and scalar and residual dipolar couplings. The polypeptide fold comprises six regions of alpha-helical secondary structure that has an overall superhelical topology remotely homologous to the MIF4G homology domain of the human nuclear cap binding protein 80 kDa subunit and the VHS domain of the Drosophila protein Hrs, though strict analysis of the structures suggests that these domains are not functionally related. Two prominent hydrophobic pockets in the gap between helices alpha2 and alpha4 suggest a potential ligand-binding characteristic for this globular domain.
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{{ABSTRACT_PUBMED_14672664}}
==About this Structure==
==About this Structure==
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1Q2Z is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q2Z OCA].
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1Q2Z is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q2Z OCA].
==Reference==
==Reference==
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[[Category: Nmr spectroscopy]]
[[Category: Nmr spectroscopy]]
[[Category: Protein structure]]
[[Category: Protein structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:48:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:17:36 2008''

Revision as of 05:17, 29 July 2008

Image:1q2z.png

Template:STRUCTURE 1q2z

The 3D solution structure of the C-terminal region of Ku86

Template:ABSTRACT PUBMED 14672664

About this Structure

1Q2Z is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

The 3D solution structure of the C-terminal region of Ku86 (Ku86CTR)., Harris R, Esposito D, Sankar A, Maman JD, Hinks JA, Pearl LH, Driscoll PC, J Mol Biol. 2004 Jan 9;335(2):573-82. PMID:14672664

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