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Solution structure of the CD3epsilondelta ectodomain and comparison with CD3epsilongamma as a basis for modeling T cell receptor topology and signaling.

Invariant CD3 subunit dimers (CD3[epsilon][gamma] CD3[epsilon][delta], and CD3[zeta][zeta]) are the signaling components of the [alpha][beta] T cell receptor (TCR). The recently solved structure of murine CD3[epsilon][gamma] revealed a unique side-to-side interface and central [beta]-sheets conjoine... Full description

Journal Title: Proceedings of the National Academy of Sciences of the United States of America November 30, 2004, Vol.101(48), pp.16867-16872
Main Author: Sun, Zhen-Yu J
Other Authors: Kim, Sun Taek , Kim, Il Chul , Fahmy, Amr , Reinherz, Ellis L , Wagner, Gerhard
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0027-8424
Link: http://search.proquest.com/docview/67137625/?pq-origsite=primo
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title: Solution structure of the CD3epsilondelta ectodomain and comparison with CD3epsilongamma as a basis for modeling T cell receptor topology and signaling.
format: Article
creator:
  • Sun, Zhen-Yu J
  • Kim, Sun Taek
  • Kim, Il Chul
  • Fahmy, Amr
  • Reinherz, Ellis L
  • Wagner, Gerhard
subjects:
  • Amino Acid Sequence–Chemistry
  • Animals–Genetics
  • Cd3 Complex–Metabolism
  • Dimerization–Chemistry
  • Glycosylation–Metabolism
  • Mice–Metabolism
  • Models, Molecular–Metabolism
  • Molecular Sequence Data–Metabolism
  • Nuclear Magnetic Resonance, Biomolecular–Metabolism
  • Protein Conformation–Metabolism
  • Receptors, Antigen, T-Cell–Metabolism
  • Signal Transduction–Metabolism
  • Solutions–Metabolism
  • Cd3 Complex
  • Receptors, Antigen, T-Cell
  • Solutions
ispartof: Proceedings of the National Academy of Sciences of the United States of America, November 30, 2004, Vol.101(48), pp.16867-16872
description: Invariant CD3 subunit dimers (CD3[epsilon][gamma] CD3[epsilon][delta], and CD3[zeta][zeta]) are the signaling components of the [alpha][beta] T cell receptor (TCR). The recently solved structure of murine CD3[epsilon][gamma] revealed a unique side-to-side interface and central [beta]-sheets conjoined between the two C2-set Ig-like ectodomains, with the pairing of the parallel G strands implying a potential concerted piston-type movement for signal transduction. Although CD3[gamma], and CD3[delta] each dimerize with CD3[epsilon], there are differential CD3 subunit requirements for receptor assembly and signaling among T lineage subpopulations, presumably mandated by structural differences. Here we present the solution structure of the heterodimeric CD3[epsilon][delta] complex. Whereas the CD3[epsilon] subunit conformation is virtually identical to that in CD3[epsilon][gamma], the CD3[delta] ectodomain adopts a C1-set Ig fold, with a narrower GFC front face [beta]-sheet that is more parallel to the ABED back face than those [beta]-sheets in CD3[epsilon] and CD3[gamma] The dimer interface between CD3[delta] and CD3[epsilon] is highly conserved among species and of similar character to that in CD3[epsilon][gamma]. Glycosylation sites in CD3[delta] are arranged such that the glycans may point away from the membrane, consistent with a model of TCR assembly that allows the CD3[delta] chain to be in close contact with the TCR [alpha]-chain. This and many other structural and biological features provide a basis for modeling putative TCR/CD3 extracellular domain associations. The fact that the two clusters of transmembrane helices, namely, the three CD3[epsilon]-CD3[gamma]-TCR[beta] segments and the five CD3[epsilon]-CD3[delta]-TCR[alpha]-CD3[zeta]-CD3[zeta] segments, are presumably centered beneath the G strand-paired CD3 heterodimers has important implications for TCR signaling. single-chain C1-Ig fold | immunoreceptor tyrosine-based activation motif | NMR structure | T cell development
language: eng
source:
identifier: ISSN: 0027-8424
fulltext: fulltext
issn:
  • 00278424
  • 0027-8424
url: Link


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titleSolution structure of the CD3epsilondelta ectodomain and comparison with CD3epsilongamma as a basis for modeling T cell receptor topology and signaling.
creatorSun, Zhen-Yu J ; Kim, Sun Taek ; Kim, Il Chul ; Fahmy, Amr ; Reinherz, Ellis L ; Wagner, Gerhard
contributorSun, Zhen-Yu J (correspondence author) ; Sun, Zhen-Yu J (record owner)
ispartofProceedings of the National Academy of Sciences of the United States of America, November 30, 2004, Vol.101(48), pp.16867-16872
identifierISSN: 0027-8424
subjectAmino Acid Sequence–Chemistry ; Animals–Genetics ; Cd3 Complex–Metabolism ; Dimerization–Chemistry ; Glycosylation–Metabolism ; Mice–Metabolism ; Models, Molecular–Metabolism ; Molecular Sequence Data–Metabolism ; Nuclear Magnetic Resonance, Biomolecular–Metabolism ; Protein Conformation–Metabolism ; Receptors, Antigen, T-Cell–Metabolism ; Signal Transduction–Metabolism ; Solutions–Metabolism ; Cd3 Complex ; Receptors, Antigen, T-Cell ; Solutions
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descriptionInvariant CD3 subunit dimers (CD3[epsilon][gamma] CD3[epsilon][delta], and CD3[zeta][zeta]) are the signaling components of the [alpha][beta] T cell receptor (TCR). The recently solved structure of murine CD3[epsilon][gamma] revealed a unique side-to-side interface and central [beta]-sheets conjoined between the two C2-set Ig-like ectodomains, with the pairing of the parallel G strands implying a potential concerted piston-type movement for signal transduction. Although CD3[gamma], and CD3[delta] each dimerize with CD3[epsilon], there are differential CD3 subunit requirements for receptor assembly and signaling among T lineage subpopulations, presumably mandated by structural differences. Here we present the solution structure of the heterodimeric CD3[epsilon][delta] complex. Whereas the CD3[epsilon] subunit conformation is virtually identical to that in CD3[epsilon][gamma], the CD3[delta] ectodomain adopts a C1-set Ig fold, with a narrower GFC front face [beta]-sheet that is more parallel to the ABED back face than those [beta]-sheets in CD3[epsilon] and CD3[gamma] The dimer interface between CD3[delta] and CD3[epsilon] is highly conserved among species and of similar character to that in CD3[epsilon][gamma]. Glycosylation sites in CD3[delta] are arranged such that the glycans may point away from the membrane, consistent with a model of TCR assembly that allows the CD3[delta] chain to be in close contact with the TCR [alpha]-chain. This and many other structural and biological features provide a basis for modeling putative TCR/CD3 extracellular domain associations. The fact that the two clusters of transmembrane helices, namely, the three CD3[epsilon]-CD3[gamma]-TCR[beta] segments and the five CD3[epsilon]-CD3[delta]-TCR[alpha]-CD3[zeta]-CD3[zeta] segments, are presumably centered beneath the G strand-paired CD3 heterodimers has important implications for TCR signaling. single-chain C1-Ig fold | immunoreceptor tyrosine-based activation motif | NMR structure | T cell development
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titleSolution structure of the CD3epsilondelta ectodomain and comparison with CD3epsilongamma as a basis for modeling T cell receptor topology and signaling.
authorSun, Zhen-Yu J ; Kim, Sun Taek ; Kim, Il Chul ; Fahmy, Amr ; Reinherz, Ellis L ; Wagner, Gerhard
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