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Literature summary for 2.3.2.27 extracted from

  • Atipairin, A.; Canyuk, B.; Ratanaphan, A.
    Substitution of aspartic acid with glutamic acid at position 67 of the BRCA1 RING domain retains ubiquitin ligase activity and zinc(II) binding with a reduced transition temperature (2011), J. Biol. Inorg. Chem., 16, 217-226.
    View publication on PubMed
Search for more literature for 2.3.2.27

Application

Application Comment Organism
medicine mutation D76E has been identified in Thai familial breast cancer patients. The mutation is located in the vicinity of Zn2+ binding site II. The D67E BRCA1 RING protein assumes a preformed structure in the absence of Zn2+. The Zn2+-bound mutant protein is more folded than wild-type, resulting in enhanced proteolytic resistance and dimerization. The mutation retains Zn2+ binding, and barely perturbs the native global structure of the BRCA1 RING domain. The D67E mutation might be a neutral or mild cancer-risk modifier of other defective mechanisms underlying BRCA1-mutation-related breast cancer Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
-
 Homo sapiens

Protein Variants

Protein Variants Comment Organism
D67E mutation identified in Thai familial breast cancer patients. The mutation is located in the vicinity of Zn2+ binding site II. The D67E BRCA1 RING protein assumes a preformed structure in the absence of Zn2+. The Zn2+-bound mutant protein is more folded than wild-type, resulting in enhanced proteolytic resistance and dimerization. The mutation retains Zn2+ binding, and barely perturbs the native global structure of the BRCA1 RING domain. The D67E mutation might be a neutral or mild cancer-risk modifier of other defective mechanisms underlying BRCA1-mutation-related breast cancer Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Synonyms

Synonyms Comment Organism
BRCA1
-
 Homo sapiens
breast cancer susceptibility protein 1
-
 Homo sapiens