Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Structural and thermodynamic correlates of t cell signaling

Academic Article
uri icon
  • Overview
  • Research
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Rudolph, M. G.
  • Luz, J. G.
  • Wilson, Ian

publication date

  • 2002

journal

  • Annual Review of Biophysics and Biomolecular Structure  Journal

abstract

  • The first crystal structures of intact T cell receptors (TCRs) bound to class I peptide-MHC (pMHCs) antigens were determined in 1996. Since then, further structures of class I TCR/pMHC complexes have explored the degree of structural variability in the TCR-pMHC system and the structural basis for positive and negative selection. The recent determination of class II and allogeneic class I TCR/pMHC structures, as well as those of accessory molecules (e.g., CD3), has pushed our knowledge of TCR/pMHC interactions into new realms, shedding light on clinical pathologies, such as graft rejection and graft-versus-host disease. Furthermore, the determination of coreceptor structures lays the foundation for a more comprehensive structural description of the supramolecular TCR signaling events and those assemblies that arise in the immunological synapse. While these telling photodocumentaries of the TCR/pMHC interaction are composed mainly from static crystal structures, a full description of the biological snapshots in T cell signaling requires additional analytical methods that record the dynamics of the process. To this end, surface plasmon resonance (SPR), isothermal titration calorimetry (ITC), and ultracentrifugation (UC) have furnished both affinities and kinetics of the TCR/pMHC association. In the past year, structural, biochemical, and molecular biological data describing TCR/pMHC interactions have sublimely coalesced into a burgeoning well of understanding that promises to deliver further insights into T cell recognition. The coming years will, through a more intimate union of structural and kinetic data, allow many pressing questions to be addressed, such as how TCR/pMHC ligation is affected by coreceptor binding and what is the mechanism of TCR signaling in both early and late stages of T cell engagement with antigen-presenting cells.

subject areas

  • Animals
  • Crystallography, X-Ray
  • Humans
  • Kinetics
  • Major Histocompatibility Complex
  • Models, Molecular
  • Protein Binding
  • Signal Transduction
  • Structure-Activity Relationship
  • T-Lymphocytes
  • Thermodynamics
scroll to property group menus

Research

keywords

  • T cell receptor
  • coreceptors
  • crystal structure
  • immunological synapse
  • major histocompatibility complex
  • protein-protein interaction
  • thermodynamic and kinetic properties
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 1056-8700

Digital Object Identifier (DOI)

  • 10.1146/annurev.biophys.31.082901.134423

PubMed ID

  • 11988465
scroll to property group menus

Additional Document Info

start page

  • 121

end page

  • 149

volume

  • 31

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support