1iea
From Proteopedia
(New page: 200px<br /><applet load="1iea" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iea, resolution 2.3Å" /> '''HISTOCOMPATIBILITY AN...) |
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- | [[Image:1iea.gif|left|200px]]<br /><applet load="1iea" size=" | + | [[Image:1iea.gif|left|200px]]<br /><applet load="1iea" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1iea, resolution 2.3Å" /> | caption="1iea, resolution 2.3Å" /> | ||
'''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== | ||
- | 1IEA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1IEA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IEA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
- | [[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 11:10, 21 February 2008
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HISTOCOMPATIBILITY ANTIGEN
Overview
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
1IEA is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 13:10:58 2008