1tcr: Difference between revisions

Revision as of 16:12, 21 February 2008

MURINE T-CELL ANTIGEN RECEPTOR 2C CLONE

OverviewOverview

The central event in the cellular immune response to invading microorganisms is the specific recognition of foreign peptides bound to major histocompatibility complex (MHC) molecules by the alphabeta T cell receptor (TCR). The x-ray structure of the complete extracellular fragment of a glycosylated alphabeta TCR was determined at 2.5 angstroms, and its orientation bound to a class I MHC-peptide (pMHC) complex was elucidated from crystals of the TCR-pMHC complex. The TCR resembles an antibody in the variable Valpha and Vbeta domains but deviates in the constant Calpha domain and in the interdomain pairing of Calpha with Cbeta. Four of seven possible asparagine-linked glycosylation sites have ordered carbohydrate moieties, one of which lies in the Calpha-Cbeta interface. The TCR combining site is relatively flat except for a deep hydrophobic cavity between the hypervariable CDR3s (complementarity-determining regions) of the alpha and beta chains. The 2C TCR covers the class I MHC H-2Kb binding groove so that the Valpha CDRs 1 and 2 are positioned over the amino-terminal region of the bound dEV8 peptide, the Vbeta chain CDRs 1 and 2 are over the carboxyl-terminal region of the peptide, and the Valpha and Vbeta CDR3s straddle the peptide between the helices around the central position of the peptide.

About this StructureAbout this Structure

1TCR is a Protein complex structure of sequences from Mus musculus with and as ligands. The following page contains interesting information on the relation of 1TCR with [Major Histocompatibility Complex]. Full crystallographic information is available from OCA.

ReferenceReference

An alphabeta T cell receptor structure at 2.5 A and its orientation in the TCR-MHC complex., Garcia KC, Degano M, Stanfield RL, Brunmark A, Jackson MR, Peterson PA, Teyton L, Wilson IA, Science. 1996 Oct 11;274(5285):209-19. PMID:8824178

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OCA

@@ Line 4: / Line 4: @@
 ==Overview==
-The central event in the cellular immune response to invading, microorganisms is the specific recognition of foreign peptides bound to, major histocompatibility complex (MHC) molecules by the alphabeta T cell, receptor (TCR). The x-ray structure of the complete extracellular fragment, of a glycosylated alphabeta TCR was determined at 2.5 angstroms, and its, orientation bound to a class I MHC-peptide (pMHC) complex was elucidated, from crystals of the TCR-pMHC complex. The TCR resembles an antibody in, the variable Valpha and Vbeta domains but deviates in the constant Calpha, domain and in the interdomain pairing of Calpha with Cbeta. Four of seven, possible asparagine-linked glycosylation sites have ordered carbohydrate, moieties, one of which lies in the Calpha-Cbeta interface. The TCR, combining site is relatively flat except for a deep hydrophobic cavity, between the hypervariable CDR3s (complementarity-determining regions) of, the alpha and beta chains. The 2C TCR covers the class I MHC H-2Kb binding, groove so that the Valpha CDRs 1 and 2 are positioned over the, amino-terminal region of the bound dEV8 peptide, the Vbeta chain CDRs 1, and 2 are over the carboxyl-terminal region of the peptide, and the Valpha, and Vbeta CDR3s straddle the peptide between the helices around the, central position of the peptide.
+The central event in the cellular immune response to invading microorganisms is the specific recognition of foreign peptides bound to major histocompatibility complex (MHC) molecules by the alphabeta T cell receptor (TCR). The x-ray structure of the complete extracellular fragment of a glycosylated alphabeta TCR was determined at 2.5 angstroms, and its orientation bound to a class I MHC-peptide (pMHC) complex was elucidated from crystals of the TCR-pMHC complex. The TCR resembles an antibody in the variable Valpha and Vbeta domains but deviates in the constant Calpha domain and in the interdomain pairing of Calpha with Cbeta. Four of seven possible asparagine-linked glycosylation sites have ordered carbohydrate moieties, one of which lies in the Calpha-Cbeta interface. The TCR combining site is relatively flat except for a deep hydrophobic cavity between the hypervariable CDR3s (complementarity-determining regions) of the alpha and beta chains. The 2C TCR covers the class I MHC H-2Kb binding groove so that the Valpha CDRs 1 and 2 are positioned over the amino-terminal region of the bound dEV8 peptide, the Vbeta chain CDRs 1 and 2 are over the carboxyl-terminal region of the peptide, and the Valpha and Vbeta CDR3s straddle the peptide between the helices around the central position of the peptide.
 ==About this Structure==
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 [[Category: Protein complex]]
 [[Category: Degano, M.]]
-[[Category: Garcia, K.C.]]
+[[Category: Garcia, K C.]]
-[[Category: Stanfield, R.L.]]
+[[Category: Stanfield, R L.]]
-[[Category: Wilson, I.A.]]
+[[Category: Wilson, I A.]]
 [[Category: NAG]]
 [[Category: SO4]]
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 [[Category: transmembrane]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:56:16 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:12:10 2008''