3D structure of transporter associated with antigen processing (TAP) obtained by single particle image analysis

G Velarde, R Ford, M F Rosenberg, Simon John Powis

Research output: Contribution to journalArticlepeer-review

34 Citations (Scopus)

Abstract

dThe transporter associated with antigen processing (TAP) is an ATP binding cassette transporter responsible for peptide translocation into the lumen of the endoplasmic reticulum for assembly with major histocompatibility complex class I molecules. Immunoaffinity-purified TAP particles comprising TAP1 and TAP2 polypeptides, and TAP2 particles alone were characterized after detergent solubilization and studied by electron microscopy. Projection structures of TAP1+2 particles reveal a molecule similar to 10 nm across with a deeply staining central region, whereas TAP2 molecules are smaller in projection. A three-dimensional structure of TAP reveals it is isolated as a single heterodimeric complex, with the TAP1 and TAP2 subunits combining to create a central 3-nm-diameter pocket on the predicted endoplasmic reticulum-lumenal side, Its structural similarity to other ABC transporters demonstrates a common tertiary structure for this diverse family of membrane proteins.

Original languageEnglish
Pages (from-to)46054-46063
Number of pages10
JournalJournal of Biological Chemistry
Volume276
Issue number49
DOIs
Publication statusPublished - 7 Dec 2001

Keywords

  • CLASS-I MOLECULES
  • MAJOR HISTOCOMPATIBILITY COMPLEX
  • PUTATIVE PEPTIDE TRANSPORTER
  • MHC-LINKED TRANSPORTER
  • ABC TRANSPORTER
  • ELECTRON-MICROSCOPY
  • NUCLEOTIDE-BINDING
  • MEMBRANE TOPOLOGY
  • CRYSTAL-STRUCTURE
  • ESCHERICHIA-COLI

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