ArticleBiochemistry2011
Promiscuous binding at the crossroads of numerous cancer pathways: insight from the binding of glutaminase interacting protein with glutaminase L.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Blocking the functional domain of TIP1 by antibodies sensitizes cancer to radiation therapy.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2023Article
- PDZ Domain Recognition: Insight from Human Tax-Interacting Protein 1 (TIP-1) Interaction with Target Proteins.Biology · 2015Review
- New partner proteins containing novel internal recognition motif for human glutaminase interacting protein (hGIP).Biochemical and biophysical research communications · 2013Article
- Specificity and promiscuity in human glutaminase interacting protein recognition: insight from the binding of the internal and C-terminal motif.Biochemistry · 2012Article
- Identification of brain-specific angiogenesis inhibitor 2 as an interaction partner of glutaminase interacting protein.Biochemical and biophysical research communications · 2011Article
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Authors and funding
5 authors.
Funding
Abstract
The glutaminase interacting protein (GIP) is composed of a single PDZ domain that interacts with a growing list of partner proteins, including glutaminase L, that are involved in a number of cell signaling and cancer pathways. Therefore, GIP makes a good target for structure-based drug design. Here, we report the solution structures of both free GIP and GIP bound to the C-terminal peptide analogue of glutaminase L. This is the first reported nuclear magnetic resonance structure of GIP in a complex with one of its binding partners. Our analysis of both free GIP and GIP in a complex with the glutaminase L peptide provides important insights into how a promiscuous binding domain can have affinity for multiple binding partners. Through a detailed chemical shift perturbation analysis and backbone dynamics studies, we demonstrate here that the binding of the glutaminase L peptide to GIP is an allosteric event. Taken together, the insights reported here lay the groundwork for the future development of a specific inhibitor for GIP.
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Registered trials
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