2vlk
From Proteopedia
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caption="2vlk, resolution 2.50Å" /> | caption="2vlk, resolution 2.50Å" /> | ||
'''THE STRUCTURAL DYNAMICS AND ENERGETICS OF AN IMMUNODOMINANT T-CELL RECEPTOR ARE PROGRAMMED BY ITS VBETA DOMAIN'''<br /> | '''THE STRUCTURAL DYNAMICS AND ENERGETICS OF AN IMMUNODOMINANT T-CELL RECEPTOR ARE PROGRAMMED BY ITS VBETA DOMAIN'''<br /> | ||
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| + | ==Overview== | ||
| + | Immunodominant and public T cell receptor (TCR) usage is relatively common in many viral diseases yet surprising in the context of the large naive TCR repertoire. We examined the highly conserved Vbeta17:Valpha10.2 JM22 T cell response to the influenza matrix peptide (58-66)-HLA-A( *)0201 (HLA-A2-flu) through extensive kinetic, thermodynamic, and structural analyses. We found several conformational adjustments that accompany JM22-HLA-A2-flu binding and identified a binding "hotspot" within the Vbeta domain of the TCR. Within this hotspot, key germline-encoded CDR1 and CDR2 loop residues and a crucial but commonly coded residue in the hypervariable region of CDR3 provide the basis for the substantial bias in the selection of the germline-encoded Vbeta17 domain. The chances of having a substantial number of T cells in the naive repertoire that have HLA-A2-flu-specific Vbeta17 receptors may consequently be relatively high, thus explaining the immunodominant usage of this clonotype. | ||
==About this Structure== | ==About this Structure== | ||
2VLK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VLK OCA]. | 2VLK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VLK OCA]. | ||
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| + | ==Reference== | ||
| + | The structural dynamics and energetics of an immunodominant T cell receptor are programmed by its Vbeta domain., Ishizuka J, Stewart-Jones GB, van der Merwe A, Bell JI, McMichael AJ, Jones EY, Immunity. 2008 Feb;28(2):171-82. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18275829 18275829] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: ubl conjugation]] | [[Category: ubl conjugation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 27 07:48:28 2008'' |
Revision as of 05:48, 27 February 2008
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THE STRUCTURAL DYNAMICS AND ENERGETICS OF AN IMMUNODOMINANT T-CELL RECEPTOR ARE PROGRAMMED BY ITS VBETA DOMAIN
Overview
Immunodominant and public T cell receptor (TCR) usage is relatively common in many viral diseases yet surprising in the context of the large naive TCR repertoire. We examined the highly conserved Vbeta17:Valpha10.2 JM22 T cell response to the influenza matrix peptide (58-66)-HLA-A( *)0201 (HLA-A2-flu) through extensive kinetic, thermodynamic, and structural analyses. We found several conformational adjustments that accompany JM22-HLA-A2-flu binding and identified a binding "hotspot" within the Vbeta domain of the TCR. Within this hotspot, key germline-encoded CDR1 and CDR2 loop residues and a crucial but commonly coded residue in the hypervariable region of CDR3 provide the basis for the substantial bias in the selection of the germline-encoded Vbeta17 domain. The chances of having a substantial number of T cells in the naive repertoire that have HLA-A2-flu-specific Vbeta17 receptors may consequently be relatively high, thus explaining the immunodominant usage of this clonotype.
About this Structure
2VLK is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The structural dynamics and energetics of an immunodominant T cell receptor are programmed by its Vbeta domain., Ishizuka J, Stewart-Jones GB, van der Merwe A, Bell JI, McMichael AJ, Jones EY, Immunity. 2008 Feb;28(2):171-82. PMID:18275829
Page seeded by OCA on Wed Feb 27 07:48:28 2008
Categories: Homo sapiens | Protein complex | Bell, J. | Ishizuka, J. | Jones, Y. | Mcmichael, A. | Merwe, A Van Der. | Stewart-Jones, G. | Complex | Disease mutation | Flu | Glycation | Glycoprotein | Host-virus interaction | Immune response | Immune system/receptor/complex | Immunodominance | Immunoglobulin domain | Membrane | Mhc | Mhc i | Peptide | Polymorphism | Pyrrolidone carboxylic acid | Receptor | Secreted | T-cell | Tcr | Transmembrane | Ubl conjugation
