2L4T: GIP/Glutaminase L peptide complex

Citation:
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.
PDB ID: 2L4TDownload
MMDB ID: 89625
PDB Deposition Date: 2010/10/13
Updated in MMDB: 2012/10
Experimental Method:
solution nmr
Source Organism:
Homo sapiens
Similar Structures:
Biological Unit for 2L4T: dimeric; determined by author
Molecular Components in 2L4T
Label Count Molecule
Proteins (2 molecules)
1
Tax1-binding Protein 3(Gene symbol: TAX1BP3)
Molecule annotation
1
Glutaminase L Peptide
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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