PDBsum entry 3k15

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Protein binding PDB id
Protein chain
211 a.a. *
Waters ×19
* Residue conservation analysis
PDB id:
Name: Protein binding
Title: Crystal structure of brca1 brct d1840t in complex with a min recognition tetrapeptide with an amidated c-terminus
Structure: Breast cancer type 1 susceptibility protein. Chain: a. Fragment: brct domain (unp residues 1646 to 1859). Synonym: ring finger protein 53. Engineered: yes. Mutation: yes. Phospho peptide. Chain: b. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: brca1, rnf53. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: sequence occurs naturally in humans in the bach1/brip1 protein. Synthesized by the alberta peptide ins
2.80Å     R-factor:   0.252     R-free:   0.280
Authors: S.J.Campbell,R.A.Edwards,J.N.Glover
Key ref: S.J.Campbell et al. (2010). Comparison of the structures and peptide binding specificities of the BRCT domains of MDC1 and BRCA1. Structure, 18, 167-176. PubMed id: 20159462
25-Sep-09     Release date:   02-Mar-10    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P38398  (BRCA1_HUMAN) -  Breast cancer type 1 susceptibility protein
1863 a.a.
211 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     nucleus   1 term 
  Biological process     DNA repair   1 term 
  Biochemical function     DNA binding     3 terms  


Structure 18:167-176 (2010)
PubMed id: 20159462  
Comparison of the structures and peptide binding specificities of the BRCT domains of MDC1 and BRCA1.
S.J.Campbell, R.A.Edwards, J.N.Glover.
The tandem BRCT domains of BRCA1 and MDC1 facilitate protein signaling at DNA damage foci through specific interactions with serine-phosphorylated protein partners. The MDC1 BRCT binds pSer-Gln-Glu-Tyr-COO(-) at the C terminus of the histone variant gammaH2AX via direct recognition of the C-terminal carboxylate, while BRCA1 recognizes pSer-X-X-Phe motifs either at C-terminal or internal sites within target proteins. Using fluorescence polarization binding assays, we show that while both BRCTs prefer a free main chain carboxylate at the +3 position, this preference is much more pronounced in MDC1. Crystal structures of BRCA1 and MDC1 bound to tetrapeptide substrates reveal differences in the environment of conserved arginines (Arg1699 in BRCA1 and Arg1933 in MDC1) that determine the relative affinity for peptides with -COO(-) versus -CO-NH(2) termini. A mutation in MDC1 that induces a more BRCA1-like conformation relaxes the binding specificity, allowing the mutant to bind phosphopeptides lacking a -COO(-) terminus.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20607147 D.Ray, A.M.Nyong, and A.Natarajan (2010).
Synthesis of unnatural amino acid derivatives via palladium catalyzed 1,4 addition of boronic acids.
  Tetrahedron Lett, 51, 2655-2656.  
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