1fyt: Difference between revisions

Revision as of 13:44, 21 February 2008

CRYSTAL STRUCTURE OF A COMPLEX OF A HUMAN ALPHA/BETA-T CELL RECEPTOR, INFLUENZA HA ANTIGEN PEPTIDE, AND MHC CLASS II MOLECULE, HLA-DR1

OverviewOverview

An alphabeta T-cell receptor (alphabetaTCR)/hemagglutinin (HA) peptide/human leukocyte antigen (HLA)-DR1 complex was stabilized by flexibly linking the HA peptide with the human HA1.7 alphabetaTCR, to increase the local concentration of the interacting proteins once the peptide has been loaded onto the major histocompatibility complex (MHC) molecule. The structure of the complex, determined by X-ray crystallography, has a binding mode similar to that of the human B7 alphabetaTCR on a pMHCI molecule. Twelve of the 15 MHC residues contacted are at the same positions observed earlier in class I MHC/peptide/TCR complexes. One contact, to an MHC loop outside the peptide-binding site, is conserved and specific to pMHCII complexes. TCR gene usage in the response to HA/HLA-DR appears to conserve charged interactions between three lysines of the peptide and acidic residues on the TCR.

About this StructureAbout this Structure

1FYT is a Protein complex structure of sequences from Homo sapiens and Influenza a virus (a/hong kong(h3n2)) with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structure of a covalently stabilized complex of a human alphabeta T-cell receptor, influenza HA peptide and MHC class II molecule, HLA-DR1., Hennecke J, Carfi A, Wiley DC, EMBO J. 2000 Nov 1;19(21):5611-24. PMID:11060013

Page seeded by OCA on Thu Feb 21 12:44:04 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1fyt.gif|left|200px]]<br />
+[[Image:1fyt.gif|left|200px]]<br /><applet load="1fyt" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1fyt" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1fyt, resolution 2.60&Aring;" />
 '''CRYSTAL STRUCTURE OF A COMPLEX OF A HUMAN ALPHA/BETA-T CELL RECEPTOR, INFLUENZA HA ANTIGEN PEPTIDE, AND MHC CLASS II MOLECULE, HLA-DR1'''<br />
 ==Overview==
-An alphabeta T-cell receptor (alphabetaTCR)/hemagglutinin (HA), peptide/human leukocyte antigen (HLA)-DR1 complex was stabilized by, flexibly linking the HA peptide with the human HA1.7 alphabetaTCR, to, increase the local concentration of the interacting proteins once the, peptide has been loaded onto the major histocompatibility complex (MHC), molecule. The structure of the complex, determined by X-ray, crystallography, has a binding mode similar to that of the human B7, alphabetaTCR on a pMHCI molecule. Twelve of the 15 MHC residues contacted, are at the same positions observed earlier in class I MHC/peptide/TCR, complexes. One contact, to an MHC loop outside the peptide-binding site, is conserved and specific to pMHCII complexes. TCR gene usage in the, response to HA/HLA-DR appears to conserve charged interactions between, three lysines of the peptide and acidic residues on the TCR.
+An alphabeta T-cell receptor (alphabetaTCR)/hemagglutinin (HA) peptide/human leukocyte antigen (HLA)-DR1 complex was stabilized by flexibly linking the HA peptide with the human HA1.7 alphabetaTCR, to increase the local concentration of the interacting proteins once the peptide has been loaded onto the major histocompatibility complex (MHC) molecule. The structure of the complex, determined by X-ray crystallography, has a binding mode similar to that of the human B7 alphabetaTCR on a pMHCI molecule. Twelve of the 15 MHC residues contacted are at the same positions observed earlier in class I MHC/peptide/TCR complexes. One contact, to an MHC loop outside the peptide-binding site, is conserved and specific to pMHCII complexes. TCR gene usage in the response to HA/HLA-DR appears to conserve charged interactions between three lysines of the peptide and acidic residues on the TCR.
 ==About this Structure==
-FYT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/hong_kong(h3n2)) Influenza a virus (a/hong kong(h3n2))] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FYT OCA].
+FYT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/hong_kong(h3n2)) Influenza a virus (a/hong kong(h3n2))] 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=1FYT OCA].
 ==Reference==
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 [[Category: Carfi, A.]]
 [[Category: Hennecke, J.]]
-[[Category: Wiley, D.C.]]
+[[Category: Wiley, D C.]]
 [[Category: NAG]]
 [[Category: immunoglobulin fold]]
 [[Category: protein-protein complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:58:26 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:44:04 2008''