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Structure paper

TitleComparison of the Structures and Peptide Binding Specificities of the BRCT Domains of MDC1 and BRCA1
Journal, issue, pagesStructure, Vol. 18, Page 167-176, Year 2010
Publish dateSep 24, 2009 (structure data deposition date)
AuthorsCampbell, S.J. / Edwards, R.A. / Glover, J.N.
External linksStructure / PubMed:20159462
MethodsX-ray diffraction
Resolution1.33 - 3 Å
Structure data

PDB-3k05:
The crystal structure of MDC1 BRCT T2067D in complex with a minimal recognition tetrapeptide with an amidated C-terminus
Method: X-RAY DIFFRACTION / Resolution: 1.33 Å

PDB-3k0h:
The crystal structure of BRCA1 BRCT in complex with a minimal recognition tetrapeptide with an amidated C-terminus
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-3k0k:
Crystal Structure of BRCA1 BRCT in complex with a minimal recognition tetrapeptide with a free carboxy C-terminus.
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-3k15:
Crystal Structure of BRCA1 BRCT D1840T in complex with a minimal recognition tetrapeptide with an amidated C-terminus
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-3k16:
Crystal Structure of BRCA1 BRCT D1840T in complex with a minimal recognition tetrapeptide with a free carboxy C-terminus
Method: X-RAY DIFFRACTION / Resolution: 3 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-NI:
NICKEL (II) ION

ChemComp-CL:
Unknown entry

Source
  • homo sapiens (human)
KeywordsPROTEIN BINDING / BRCT Domain / protein-peptide complex / phospho protein binding / H2AX / DNA damage response / Cell cycle / DNA damage / DNA repair / Nucleus / Phosphoprotein / BRCA1 / phospho peptide interactions / BACH1 / Alternative initiation / Disease mutation / DNA-binding / Fatty acid biosynthesis / Ligase / Lipid synthesis / Metal-binding / Tumor suppressor / Ubl conjugation pathway / Zinc-finger / Abraxas / ISOMERASE

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