PMID- 19609323
OWN - NLM
STAT- MEDLINE
DCOM- 20091110
LR  - 20220129
IS  - 1469-3178 (Electronic)
IS  - 1469-221X (Print)
IS  - 1469-221X (Linking)
VI  - 10
IP  - 9
DP  - 2009 Sep
TI  - Structural basis for recruitment of BRCA2 by PALB2.
PG  - 990-6
LID - 10.1038/embor.2009.126 [doi]
AB  - The breast cancer 2, early onset protein (BRCA2) is central to the repair of DNA 
      damage by homologous recombination. BRCA2 recruits the recombinase RAD51 to sites 
      of damage, regulates its assembly into nucleoprotein filaments and thereby 
      promotes homologous recombination. Localization of BRCA2 to nuclear foci requires 
      its association with the partner and localizer of BRCA2 (PALB2), mutations in 
      which are associated with cancer predisposition, as well as subtype N of Fanconi 
      anaemia. We have determined the structure of the PALB2 carboxy-terminal 
      beta-propeller domain in complex with a BRCA2 peptide. The structure shows the 
      molecular determinants of this important protein-protein interaction and explains 
      the effects of both cancer-associated truncating mutants in PALB2 and missense 
      mutations in the amino-terminal region of BRCA2.
FAU - Oliver, Antony W
AU  - Oliver AW
AD  - Cancer Research UK DNA Repair Enzymes Group, Section of Structural Biology, 237 
      Fulham Road, London SW3 6JB, UK. antony.oliver@icr.ac.uk
FAU - Swift, Sally
AU  - Swift S
FAU - Lord, Christopher J
AU  - Lord CJ
FAU - Ashworth, Alan
AU  - Ashworth A
FAU - Pearl, Laurence H
AU  - Pearl LH
LA  - eng
SI  - PDB/2W18
SI  - PDB/3EU7
GR  - A8363/CRUK_/Cancer Research UK/United Kingdom
GR  - BREAST CANCER NOW RESEARCH CENTRE/BCN_/Breast Cancer Now/United Kingdom
GR  - C302/A7803/CRUK_/Cancer Research UK/United Kingdom
GR  - C302/A8265/CRUK_/Cancer Research UK/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20090717
PL  - England
TA  - EMBO Rep
JT  - EMBO reports
JID - 100963049
RN  - 0 (Apoptosis Regulatory Proteins)
RN  - 0 (BLID protein, human)
RN  - 0 (BRCA2 Protein)
RN  - 0 (BRCA2 protein, human)
RN  - 0 (Fanconi Anemia Complementation Group N Protein)
RN  - 0 (Nuclear Proteins)
RN  - 0 (PALB2 protein, human)
RN  - 0 (Tumor Suppressor Proteins)
SB  - IM
EIN - EMBO Rep. 2017 Jul;18(7):1264. PMID: 28673926
MH  - Amino Acid Sequence
MH  - Animals
MH  - Apoptosis Regulatory Proteins
MH  - BRCA2 Protein/*chemistry/genetics/*metabolism
MH  - Binding Sites
MH  - Cell Line
MH  - Crystallography, X-Ray
MH  - Fanconi Anemia Complementation Group N Protein
MH  - Humans
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Nuclear Proteins/*chemistry/genetics/*metabolism
MH  - Protein Binding
MH  - Protein Structure, Quaternary
MH  - Protein Structure, Tertiary
MH  - Sequence Alignment
MH  - Tumor Suppressor Proteins/*chemistry/genetics/*metabolism
PMC - PMC2750052
COIS- The authors declare that they have no conflict of interest.
EDAT- 2009/07/18 09:00
MHDA- 2009/11/11 06:00
PMCR- 2010/09/01
CRDT- 2009/07/18 09:00
PHST- 2009/03/04 00:00 [received]
PHST- 2009/04/30 00:00 [revised]
PHST- 2009/05/05 00:00 [accepted]
PHST- 2009/07/18 09:00 [entrez]
PHST- 2009/07/18 09:00 [pubmed]
PHST- 2009/11/11 06:00 [medline]
PHST- 2010/09/01 00:00 [pmc-release]
AID - embor2009126 [pii]
AID - 10.1038/embor.2009.126 [doi]
PST - ppublish
SO  - EMBO Rep. 2009 Sep;10(9):990-6. doi: 10.1038/embor.2009.126. Epub 2009 Jul 17.