Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3

Dachuan Zhang, Anatoly Kiyatkin, Jeffrey T. Bolin, Philip S. Low

Research output: Contribution to journalArticle

251 Scopus citations

Abstract

The red blood cell membrane (RBCM) is a primary model for animal cell plasma membranes. One of its major organizing centers is the cytoplasmic domain of band 3 (cdb3), which links multiple proteins to the membrane. Included among its peripheral protein ligands are ankyrin (the major bridge to the spectrin-actin skeleton), protein 4.1, protein 4.2, aldolase, glyceraldehyde-3-phosphate dehydrogenase, phosphofructokinase, deoxyhemoglobin, p72syk protein tyrosine kinase, and hemichromes. The crystal structure of cdb3 is reported at 0.26 nm (2.6 A) resolution. A tight symmetric dimer is formed by cdb3; it is stabilized by interlocked dimerization arms contributed by both monomers. Each sub-unit also includes a larger peripheral protein binding domain with an α+ β-fold. The binding sites of several peripheral proteins are localized in the structure, and the nature of the major conformational change that regulates membrane-skeletal interactions is evaluated. An improved structural definition of the protein network at the inner surface of the RBCM is now possible. (C) 2000 by The American Society of Hematology.

Original languageEnglish (US)
Pages (from-to)2925-2933
Number of pages9
JournalBlood
Volume96
Issue number9
DOIs
StatePublished - Nov 1 2000

ASJC Scopus subject areas

  • Biochemistry
  • Immunology
  • Hematology
  • Cell Biology

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