2orl: Difference between revisions
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==Overview== | ==Overview== | ||
Protein-protein interactions are driven by specific properties of the | Protein-protein interactions are driven by specific properties of the molecular surfaces. Cytochrome c, a small electron transfer protein, is involved in a number of biologically relevant interactions with macromolecular partners. Small molecules may interfere with such interactions by binding to the surface of cytochrome c. Here we investigated the possibility of weak intermolecular interactions between reduced cytochrome c and a library of 325 small molecules, using WaterLOGSY NMR spectroscopy. Specific binding was found for p-aminophenol. The solution structure of the p-aminophenol-cytochrome c adduct was determined using a combination of in silico tools and NMR-based restraints. The ligand interacts in a specific binding site on the protein surface through a combination of stacking and H-bond interactions. Small but meaningful rearrangements of the solvent-exposed side chains are observed upon ligand binding and contribute to the stabilization of the complex. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Assfalg, M.]] | [[Category: Assfalg, M.]] | ||
[[Category: Bertini, I.]] | [[Category: Bertini, I.]] | ||
[[Category: Conte, R | [[Category: Conte, R Del.]] | ||
[[Category: Giachetti, A.]] | [[Category: Giachetti, A.]] | ||
[[Category: Turano, P.]] | [[Category: Turano, P.]] | ||
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[[Category: protein-ligand adduct]] | [[Category: protein-ligand adduct]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:21:46 2008'' | ||
Revision as of 19:21, 21 February 2008
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Solution structure of the cytochrome c- para-aminophenol adduct
OverviewOverview
Protein-protein interactions are driven by specific properties of the molecular surfaces. Cytochrome c, a small electron transfer protein, is involved in a number of biologically relevant interactions with macromolecular partners. Small molecules may interfere with such interactions by binding to the surface of cytochrome c. Here we investigated the possibility of weak intermolecular interactions between reduced cytochrome c and a library of 325 small molecules, using WaterLOGSY NMR spectroscopy. Specific binding was found for p-aminophenol. The solution structure of the p-aminophenol-cytochrome c adduct was determined using a combination of in silico tools and NMR-based restraints. The ligand interacts in a specific binding site on the protein surface through a combination of stacking and H-bond interactions. Small but meaningful rearrangements of the solvent-exposed side chains are observed upon ligand binding and contribute to the stabilization of the complex.
About this StructureAbout this Structure
2ORL is a Single protein structure of sequence from Saccharomyces cerevisiae with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Cytochrome c and organic molecules: solution structure of the p-aminophenol adduct., Assfalg M, Bertini I, Del Conte R, Giachetti A, Turano P, Biochemistry. 2007 May 29;46(21):6232-8. Epub 2007 May 9. PMID:17488096
Page seeded by OCA on Thu Feb 21 18:21:46 2008