1i3r: Difference between revisions

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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]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:07:45 2008''

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@@ Line 4: / Line 4: @@
 ==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==
@@ Line 13: / Line 13: @@
 [[Category: Mus musculus]]
 [[Category: Protein complex]]
-[[Category: Kappler, J.W.]]
+[[Category: Kappler, J W.]]
 [[Category: Wilson, N.]]
 [[Category: NAG]]
@@ Line 20: / Line 20: @@
 [[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''