1i3r: Difference between revisions

Revision as of 14:07, 21 February 2008

CRYSTAL STRUCTURE OF A MUTANT IEK CLASS II MHC MOLECULE

OverviewOverview

IE/DR MHC class II molecules have an extensive H-bonding network under the bound peptide. In IE(k), two alpha chain acidic amino acids in the core of this network were mutated to amides. At low pH, the mutant molecule exchanged peptide much more rapidly than the wild-type. The crystal structure of the mutant IE(k) revealed the loss of a single buried water molecule and a reorganization of the predicted H-bonding network. We suggest that these mutations enhance the transition of MHC class II to an open conformation at low pH allowing the bound peptide to escape. In wild-type IE(k), the need to protonate these amino acids also may be a bottleneck in the return to a closed conformation after peptide binding.

About this StructureAbout this Structure

1I3R is a Protein complex structure of sequences from Mus musculus with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Mutations changing the kinetics of class II MHC peptide exchange., Wilson N, Fremont D, Marrack P, Kappler J, Immunity. 2001 May;14(5):513-22. PMID:11371354

Page seeded by OCA on Thu Feb 21 13:07:45 2008

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OCA

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 ==Overview==
-IE/DR MHC class II molecules have an extensive H-bonding network under the, bound peptide. In IE(k), two alpha chain acidic amino acids in the core of, this network were mutated to amides. At low pH, the mutant molecule, exchanged peptide much more rapidly than the wild-type. The crystal, structure of the mutant IE(k) revealed the loss of a single buried water, molecule and a reorganization of the predicted H-bonding network. We, suggest that these mutations enhance the transition of MHC class II to an, open conformation at low pH allowing the bound peptide to escape. In, wild-type IE(k), the need to protonate these amino acids also may be a, bottleneck in the return to a closed conformation after peptide binding.
+IE/DR MHC class II molecules have an extensive H-bonding network under the bound peptide. In IE(k), two alpha chain acidic amino acids in the core of this network were mutated to amides. At low pH, the mutant molecule exchanged peptide much more rapidly than the wild-type. The crystal structure of the mutant IE(k) revealed the loss of a single buried water molecule and a reorganization of the predicted H-bonding network. We suggest that these mutations enhance the transition of MHC class II to an open conformation at low pH allowing the bound peptide to escape. In wild-type IE(k), the need to protonate these amino acids also may be a bottleneck in the return to a closed conformation after peptide binding.
 ==About this Structure==
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 [[Category: Mus musculus]]
 [[Category: Protein complex]]
-[[Category: Kappler, J.W.]]
+[[Category: Kappler, J W.]]
 [[Category: Wilson, N.]]
 [[Category: NAG]]
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 [[Category: peptide]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:59:27 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:07:45 2008''