2obh

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[[Image:2obh.jpg|left|200px]]<br /><applet load="2obh" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2obh.jpg|left|200px]]
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caption="2obh, resolution 1.800&Aring;" />
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'''Centrin-XPC peptide'''<br />
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{{Structure
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|PDB= 2obh |SIZE=350|CAPTION= <scene name='initialview01'>2obh</scene>, resolution 1.800&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|ACTIVITY=
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|GENE= CETN2, CALT, CEN2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Centrin-XPC peptide'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2OBH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OBH OCA].
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2OBH is a [[Protein complex]] structure of sequences 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=2OBH OCA].
==Reference==
==Reference==
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Structural, thermodynamic, and cellular characterization of human centrin 2 interaction with xeroderma pigmentosum group C protein., Charbonnier JB, Renaud E, Miron S, Le Du MH, Blouquit Y, Duchambon P, Christova P, Shosheva A, Rose T, Angulo JF, Craescu CT, J Mol Biol. 2007 Nov 2;373(4):1032-46. Epub 2007 Aug 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17897675 17897675]
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Structural, thermodynamic, and cellular characterization of human centrin 2 interaction with xeroderma pigmentosum group C protein., Charbonnier JB, Renaud E, Miron S, Le Du MH, Blouquit Y, Duchambon P, Christova P, Shosheva A, Rose T, Angulo JF, Craescu CT, J Mol Biol. 2007 Nov 2;373(4):1032-46. Epub 2007 Aug 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17897675 17897675]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: dna repair complex ef hand superfamily protein-peptide complex]]
[[Category: dna repair complex ef hand superfamily protein-peptide complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:16:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:57:30 2008''

Revision as of 15:57, 20 March 2008


PDB ID 2obh

Drag the structure with the mouse to rotate
, resolution 1.800Å
Ligands:
Gene: CETN2, CALT, CEN2 (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



Centrin-XPC peptide


Contents

Overview

Human centrin 2 (HsCen2), an EF-hand calcium binding protein, plays a regulatory role in the DNA damage recognition during the first steps of the nucleotide excision repair. This biological action is mediated by the binding to a short fragment (N847-R863) from the C-terminal region of xeroderma pigmentosum group C (XPC) protein. This work presents a detailed structural and energetic characterization of the HsCen2/XPC interaction. Using a truncated form of HsCen2 we obtained a high resolution (1.8 A) X-ray structure of the complex with the peptide N847-R863 from XPC. Structural and thermodynamic analysis of the interface revealed the existence of both electrostatic and apolar inter-molecular interactions, but the binding energy is mainly determined by the burial of apolar bulky side-chains into the hydrophobic pocket of the HsCen2 C-terminal domain. Binding studies with various peptide variants showed that XPC residues W848 and L851 constitute the critical anchoring side-chains. This enabled us to define a minimal centrin binding peptide variant of five residues, which accounts for about 75% of the total free energy of interaction between the two proteins. Immunofluorescence imaging in HeLa cells demonstrated that HsCen2 binding to the integral XPC protein may be observed in living cells, and is determined by the same interface residues identified in the X-ray structure of the complex. Overexpression of XPC perturbs the cellular distribution of HsCen2, by inducing a translocation of centrin molecules from the cytoplasm to the nucleus. The present data confirm that the in vitro structural features of the centrin/XPC peptide complex are highly relevant to the cellular context.

Disease

Known diseases associated with this structure: Xeroderma pigmentosum, group C OMIM:[278720]

About this Structure

2OBH is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural, thermodynamic, and cellular characterization of human centrin 2 interaction with xeroderma pigmentosum group C protein., Charbonnier JB, Renaud E, Miron S, Le Du MH, Blouquit Y, Duchambon P, Christova P, Shosheva A, Rose T, Angulo JF, Craescu CT, J Mol Biol. 2007 Nov 2;373(4):1032-46. Epub 2007 Aug 25. PMID:17897675

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