1ieb: Difference between revisions
New page: left|200px<br /><applet load="1ieb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ieb, resolution 2.7Å" /> '''HISTOCOMPATIBILITY AN... |
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[[Image:1ieb.gif|left|200px]]<br /><applet load="1ieb" size=" | [[Image:1ieb.gif|left|200px]]<br /><applet load="1ieb" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ieb, resolution 2.7Å" /> | caption="1ieb, resolution 2.7Å" /> | ||
'''HISTOCOMPATIBILITY ANTIGEN'''<br /> | '''HISTOCOMPATIBILITY ANTIGEN'''<br /> | ||
==Overview== | ==Overview== | ||
The high-resolution x-ray crystal structures of the murine major | 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 Structure== | ==About this Structure== | ||
1IEB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NAG, NDG and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1IEB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=NDG:'>NDG</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IEB OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Fremont, D | [[Category: Fremont, D H.]] | ||
[[Category: Hendrickson, W | [[Category: Hendrickson, W A.]] | ||
[[Category: Kappler, J.]] | [[Category: Kappler, J.]] | ||
[[Category: Marrack, P.]] | [[Category: Marrack, P.]] | ||
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[[Category: histocompatibility antigen]] | [[Category: histocompatibility antigen]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:10:58 2008'' | ||
Revision as of 14:11, 21 February 2008
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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 with , and as ligands. 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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