1nbp
From Proteopedia
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Crystal Structure Of Human Interleukin-2 Y31C Covalently Modified At C31 With 3-Mercapto-1-(1,3,4,9-tetrahydro-B-carbolin-2-yl)-propan-1-one
Contents |
Overview
The cytokine hormone interleukin-2 (IL-2) contains a highly adaptive, region that binds small, druglike molecules. The binding properties of, this adaptive region have been explored using a "tethering" method that, relies on the formation of a disulfide bond between the protein and, small-molecule ligands. Using tethering, surface plasmon resonance (SPR), and X-ray crystallography, we have discovered that the IL-2 adaptive, region contains at least two cooperative binding sites where the binding, of a first ligand to one site promotes or antagonizes the binding of a, second ligand to the second site. Cooperative energies of interaction of, -2 kcal/mol are observed. The observation that the adaptive region, contains two adjacent sites may lead to the development of tight-binding, antagonists of a protein-protein interaction. Cooperative ligand binding, in the adaptive region of IL-2 underscores the importance of protein, dynamics in molecular recognition. The tethering approach provides a novel, and general strategy for discovering such cooperative binding interactions, in specific, flexible regions of protein structure.
Disease
Known disease associated with this structure: Severe combined immunodeficiency due to IL2 deficiency OMIM:[147680]
About this Structure
1NBP is a Single protein structure of sequence from Homo sapiens with SO4 and MHC as ligands. Full crystallographic information is available from OCA.
Reference
Discovery and characterization of cooperative ligand binding in the adaptive region of interleukin-2., Hyde J, Braisted AC, Randal M, Arkin MR, Biochemistry. 2003 Jun 3;42(21):6475-83. PMID:12767230
Page seeded by OCA on Mon Nov 12 18:20:16 2007
