1xgu
From Proteopedia
(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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| - | [[Image:1xgu.gif|left|200px]]<br /> | + | [[Image:1xgu.gif|left|200px]]<br /><applet load="1xgu" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1xgu" size=" | + | |
caption="1xgu, resolution 2.10Å" /> | caption="1xgu, resolution 2.10Å" /> | ||
'''Structure for antibody HyHEL-63 Y33F mutant complexed with hen egg lysozyme'''<br /> | '''Structure for antibody HyHEL-63 Y33F mutant complexed with hen egg lysozyme'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Hydrophobic interactions are essential for stabilizing protein-protein | + | 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== | ==About this Structure== | ||
| - | 1XGU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1XGU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XGU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: 2 | + | [[Category: 2 1a crystal structure]] |
[[Category: hyhel-63]] | [[Category: hyhel-63]] | ||
[[Category: y33f mutant]] | [[Category: y33f mutant]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:54:37 2008'' |
Revision as of 13:54, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 15:54:37 2008
