2v2w: Difference between revisions
New page: left|200px<br /> <applet load="2v2w" size="450" color="white" frame="true" align="right" spinBox="true" caption="2v2w, resolution 1.60Å" /> '''T CELL CROSS-REACTI... |
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'''T CELL CROSS-REACTIVITY AND CONFORMATIONAL CHANGES DURING TCR ENGAGEMENT'''<br /> | '''T CELL CROSS-REACTIVITY AND CONFORMATIONAL CHANGES DURING TCR ENGAGEMENT'''<br /> | ||
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==Overview== | ==Overview== | ||
All thymically selected T cells are inherently cross-reactive, yet many, data indicate a fine specificity in antigen recognition, which enables, virus escape from immune control by mutation in infections such as the, human immunodeficiency virus (HIV). To address this paradox, we analyzed, the fine specificity of T cells recognizing a human histocompatibility, leukocyte antigen (HLA)-A2-restricted, strongly immunodominant, HIV gag, epitope (SLFNTVATL). The majority of 171 variant peptides tested bound, HLA-A2, but only one third were recognized. Surprisingly, one recognized, variant (SLYNTVATL) showed marked differences in structure when bound to, HLA-A2. T cell receptor (TCR) recognition of variants of these two, peptides implied that they adopted the same conformation in the, TCR-peptide-major histocompatibility complex (MHC) complex. However, the, on-rate kinetics of TCR binding were identical, implying that, conformational changes at the TCR-peptide-MHC binding interface occur, after an initial permissive antigen contact. These findings have, implications for the rational design of vaccines targeting viruses with, unstable genomes. | All thymically selected T cells are inherently cross-reactive, yet many, data indicate a fine specificity in antigen recognition, which enables, virus escape from immune control by mutation in infections such as the, human immunodeficiency virus (HIV). To address this paradox, we analyzed, the fine specificity of T cells recognizing a human histocompatibility, leukocyte antigen (HLA)-A2-restricted, strongly immunodominant, HIV gag, epitope (SLFNTVATL). The majority of 171 variant peptides tested bound, HLA-A2, but only one third were recognized. Surprisingly, one recognized, variant (SLYNTVATL) showed marked differences in structure when bound to, HLA-A2. T cell receptor (TCR) recognition of variants of these two, peptides implied that they adopted the same conformation in the, TCR-peptide-major histocompatibility complex (MHC) complex. However, the, on-rate kinetics of TCR binding were identical, implying that, conformational changes at the TCR-peptide-MHC binding interface occur, after an initial permissive antigen contact. These findings have, implications for the rational design of vaccines targeting viruses with, unstable genomes. | ||
==About this Structure== | ==About this Structure== | ||
2V2W is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure superseeds the now removed PDB entry 2BSU. Full crystallographic information is available from [http:// | 2V2W is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure superseeds the now removed PDB entry 2BSU. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V2W OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: ubl conjugation]] | [[Category: ubl conjugation]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:24:57 2008'' | ||
Revision as of 13:24, 23 January 2008
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T CELL CROSS-REACTIVITY AND CONFORMATIONAL CHANGES DURING TCR ENGAGEMENT
OverviewOverview
All thymically selected T cells are inherently cross-reactive, yet many, data indicate a fine specificity in antigen recognition, which enables, virus escape from immune control by mutation in infections such as the, human immunodeficiency virus (HIV). To address this paradox, we analyzed, the fine specificity of T cells recognizing a human histocompatibility, leukocyte antigen (HLA)-A2-restricted, strongly immunodominant, HIV gag, epitope (SLFNTVATL). The majority of 171 variant peptides tested bound, HLA-A2, but only one third were recognized. Surprisingly, one recognized, variant (SLYNTVATL) showed marked differences in structure when bound to, HLA-A2. T cell receptor (TCR) recognition of variants of these two, peptides implied that they adopted the same conformation in the, TCR-peptide-major histocompatibility complex (MHC) complex. However, the, on-rate kinetics of TCR binding were identical, implying that, conformational changes at the TCR-peptide-MHC binding interface occur, after an initial permissive antigen contact. These findings have, implications for the rational design of vaccines targeting viruses with, unstable genomes.
About this StructureAbout this Structure
2V2W is a Protein complex structure of sequences from Homo sapiens. This structure superseeds the now removed PDB entry 2BSU. Full crystallographic information is available from OCA.
ReferenceReference
T cell cross-reactivity and conformational changes during TCR engagement., Lee JK, Stewart-Jones G, Dong T, Harlos K, Di Gleria K, Dorrell L, Douek DC, van der Merwe PA, Jones EY, McMichael AJ, J Exp Med. 2004 Dec 6;200(11):1455-66. PMID:15583017
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Homo sapiens
- Protein complex
- Dong, T.
- Dorrell, L.
- Douek, D.C.
- Gleria, K.Di.
- Harlos, K.
- Jones, E.Y.
- Lee, J.K.
- Mcmichael, A.J.
- Merwe, P.A.Van.Der.
- Stewart-Jones, G.
- Aids
- Complex (antigen-peptide)
- Complex (antigen/peptide)
- Disease mutation
- Glycoprotein
- Hiv
- Hla-a2
- Host-virus interaction
- Immune response
- Immune system
- Immunoglobulin domain
- Membrane
- Mhc
- Mhc i
- Polymorphism
- Pyrrolidone carboxylic acid
- Tcr
- Transmembrane
- Ubl conjugation