1HYN

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

1HYN の概要

• エントリーDOI: 10.2210/pdb1hyn/pdb
• 分子名称: BAND 3 ANION TRANSPORT PROTEIN (2 entities in total)
• 機能のキーワード: membrane protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane ; Multi-pass membrane protein : P02730
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 170306.03

構造登録者

Zhang, D.,Kiyatkin, A.,Bolin, J.T.,Low, P.S. (登録日: 2001-01-20, 公開日: 2001-05-16, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.6 Å)