1ieb: Difference between revisions
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|PDB= 1ieb |SIZE=350|CAPTION= <scene name='initialview01'>1ieb</scene>, resolution 2.7Å | |PDB= 1ieb |SIZE=350|CAPTION= <scene name='initialview01'>1ieb</scene>, resolution 2.7Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene> | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ieb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ieb OCA], [http://www.ebi.ac.uk/pdbsum/1ieb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ieb RCSB]</span> | |||
}} | }} | ||
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[[Category: Kappler, J.]] | [[Category: Kappler, J.]] | ||
[[Category: Marrack, P.]] | [[Category: Marrack, P.]] | ||
[[Category: histocompatibility antigen]] | [[Category: histocompatibility antigen]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:18:35 2008'' | ||
Revision as of 21:18, 30 March 2008
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| , resolution 2.7Å | |||||||
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| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HISTOCOMPATIBILITY ANTIGEN
OverviewOverview
The high-resolution x-ray crystal structures of the murine major histocompatibility complex (MHC) class II molecule, I-E(k), occupied by either of two antigenic peptides were determined. They reveal the structural basis for the I-E(k) peptide binding motif and suggest general principles for additional alleles. A buried cluster of acidic amino acids in the binding groove predicted to be conserved among all murine I-E and human DR MHC class II molecules suggests how pH may influence MHC binding or exchange of peptides. These structures also complement mutational studies on the importance of individual peptide residues to T cell receptor recognition.
About this StructureAbout this Structure
1IEB is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Structures of an MHC class II molecule with covalently bound single peptides., Fremont DH, Hendrickson WA, Marrack P, Kappler J, Science. 1996 May 17;272(5264):1001-4. PMID:8638119
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