Identification of potential binding sites for the FHA domain of human Chk2 by in vitro binding studies.
Human Chk2 is a newly identified tumor suppressor protein involved in signaling pathways in response to DNA damage. The protein consists of a forkhead-associated (FHA) domain and a kinase domain. Identification of binding partners of the Chk2FHA domain is important in understanding the roles of Chk2 in signaling. We report ... development of an approach involving the use of combinatorial libraries, pull-down assays, surface plasmon resonance (SPR), and nuclear magnetic resonance (NMR) methods to identify possible candidates for the binding sites of Chk2FHA. The approach has been used to identify Thr329 of p53 and Thr1852 of breast cancer type 1 susceptibility protein (BRCA1) as very likely biological binding sites of Chk2FHA. The results provide useful leads for further biological analyses of cell signaling involving the FHA domain of Chk2 protein.
Mesh Terms:
Binding Sites, Carrier Proteins, Forkhead Transcription Factors, Humans, Nuclear Proteins, Peptide Library, Protein Binding, Protein Structure, Tertiary, Protein-Serine-Threonine Kinases, Structure-Activity Relationship, Transcription Factors, Tumor Suppressor Protein p53, Ubiquitin-Protein Ligases
Binding Sites, Carrier Proteins, Forkhead Transcription Factors, Humans, Nuclear Proteins, Peptide Library, Protein Binding, Protein Structure, Tertiary, Protein-Serine-Threonine Kinases, Structure-Activity Relationship, Transcription Factors, Tumor Suppressor Protein p53, Ubiquitin-Protein Ligases
Biochem. Biophys. Res. Commun.
Date: Nov. 28, 2003
PubMed ID: 14623252
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