TY - JOUR
T1 - Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3
AU - Zhang, Dachuan
AU - Kiyatkin, Anatoly
AU - Bolin, Jeffrey T.
AU - Low, Philip S.
PY - 2000/11/1
Y1 - 2000/11/1
N2 - 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.
AB - 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.
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U2 - 10.1182/blood.v96.9.2925
DO - 10.1182/blood.v96.9.2925
M3 - Article
C2 - 11049968
AN - SCOPUS:0034329189
VL - 96
SP - 2925
EP - 2933
JO - Blood
JF - Blood
SN - 0006-4971
IS - 9
ER -