1nbp: Difference between revisions

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[[Image:1nbp.gif|left|200px]]
{{Seed}}
[[Image:1nbp.png|left|200px]]


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{{STRUCTURE_1nbp|  PDB=1nbp  |  SCENE=  }}  
{{STRUCTURE_1nbp|  PDB=1nbp  |  SCENE=  }}  


'''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'''
===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===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_12767230}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_12767230}}


==Disease==
==Disease==
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[[Category: Four-helix bundle]]
[[Category: Four-helix bundle]]
[[Category: Small molecule complex]]
[[Category: Small molecule complex]]
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