1xgu
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(New page: 200px<br /> <applet load="1xgu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xgu, resolution 2.10Å" /> '''Structure for antib...)
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Revision as of 07:37, 18 November 2007
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Structure for antibody HyHEL-63 Y33F mutant complexed with hen egg lysozyme
Overview
Hydrophobic interactions are essential for stabilizing protein-protein, complexes, whose interfaces generally consist of a central cluster of hot, spot residues surrounded by less important peripheral residues. According, to the O-ring hypothesis, a condition for high affinity binding is solvent, exclusion from interacting residues. This hypothesis predicts that the, hydrophobicity at the center is significantly greater than at the, periphery, which we estimated at 21 cal mol(-1) A(-2). To measure the, hydrophobicity at the center, structures of an antigen-antibody complex, where a buried phenylalanine was replaced by smaller hydrophobic residues, were determined. By correlating structural changes with binding free, energies, we estimate the hydrophobicity at this central site to be 46 cal, mol(-1) A(-2), twice that at the periphery. This context dependence of the, hydrophobic effect explains the clustering of hot spots at interface, centers and has implications for hot spot prediction and the design of, small molecule inhibitors.
About this Structure
1XGU is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Magnitude of the hydrophobic effect at central versus peripheral sites in protein-protein interfaces., Li Y, Huang Y, Swaminathan CP, Smith-Gill SJ, Mariuzza RA, Structure. 2005 Feb;13(2):297-307. PMID:15698573
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