1HYN

CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF HUMAN ERYTHROCYTE BAND-3 PROTEIN

Summary for 1HYN

• Entry DOI: 10.2210/pdb1hyn/pdb
• Descriptor: BAND 3 ANION TRANSPORT PROTEIN (2 entities in total)
• Functional Keywords: membrane protein
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane ; Multi-pass membrane protein : P02730
• Total number of polymer chains: 4
• Total formula weight: 170306.03

Authors

Zhang, D.,Kiyatkin, A.,Bolin, J.T.,Low, P.S. (deposition date: 2001-01-20, release date: 2001-05-16, Last modification date: 2024-02-07)

Primary citation

Zhang, D.,Kiyatkin, A.,Bolin, J.T.,Low, P.S.
Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3.
Blood, 96:2925-2933, 2000

PubMed 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 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.

PubMed: 11049968

Experimental method

X-RAY DIFFRACTION (2.6 Å)