1i3r: Difference between revisions
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[[Image:1i3r.jpg|left|200px]] | [[Image:1i3r.jpg|left|200px]] | ||
'''CRYSTAL STRUCTURE OF A MUTANT IEK CLASS II MHC MOLECULE''' | {{Structure | ||
|PDB= 1i3r |SIZE=350|CAPTION= <scene name='initialview01'>1i3r</scene>, resolution 2.4Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene> | |||
|ACTIVITY= | |||
|GENE= IEK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |||
}} | |||
'''CRYSTAL STRUCTURE OF A MUTANT IEK CLASS II MHC MOLECULE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1I3R is a [ | 1I3R is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I3R OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11371354 11371354] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: peptide]] | [[Category: peptide]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:45:09 2008'' | ||
Revision as of 12:45, 20 March 2008
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| , resolution 2.4Å | |||||||
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| Ligands: | and | ||||||
| Gene: | IEK (Mus musculus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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