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

Blood. 2000 Nov 1;96(9):2925-33.


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 subunit also includes a larger peripheral protein binding domain with an alpha(+) beta-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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Anion Exchange Protein 1, Erythrocyte / chemistry*
  • Ankyrins / chemistry
  • Crystallography, X-Ray
  • Dimerization
  • Erythrocyte Membrane / chemistry
  • Humans
  • Membrane Proteins / blood
  • Membrane Proteins / chemistry
  • Models, Molecular
  • Peptide Fragments / chemistry
  • Protein Structure, Secondary
  • Protein Subunits


  • Anion Exchange Protein 1, Erythrocyte
  • Ankyrins
  • Membrane Proteins
  • Peptide Fragments
  • Protein Subunits