1OWA

Solution Structural Studies on Human Erythrocyte Alpha Spectrin N Terminal Tetramerization Domain

1OWA の概要

• エントリーDOI: 10.2210/pdb1owa/pdb
• 分子名称: Spectrin alpha chain, erythrocyte (1 entity in total)
• 機能のキーワード: triple helical bundle, cytokine
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, cytoskeleton: P02549
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18559.85

構造登録者

Park, S.,Caffrey, M.S.,Johnson, M.E.,Fung, L.W. (登録日: 2003-03-28, 公開日: 2004-03-30, 最終更新日: 2024-05-22)

主引用文献

Park, S.,Caffrey, M.S.,Johnson, M.E.,Fung, L.W.
Solution structural studies on human erythrocyte alpha-spectrin tetramerization site.
J.Biol.Chem., 278:21837-21844, 2003

PubMed Abstract: We have determined the solution NMR structure of a recombinant peptide that consists of the first 156 residues of erythroid alpha-spectrin. The first 20 residues preceding the first helix (helix C') are in a disordered conformation. The subsequent three helices (helices A1, B1, and C1) form a triple helical bundle structural domain that is similar, but not identical, to previously published structures for spectrin from Drosophila and chicken brain. Paramagnetic spin label-induced NMR resonance broadening shows that helix C', the partial domain involved in alpha- and beta-spectrin association, exhibits little interaction with the structural domain. Surprisingly, helix C' is connected to helix A1 of the structural domain by a segment of 7 residues (the junction region) that exhibits a flexible disordered conformation, in contrast to the predicted rigid helical structure. We suggest that the flexibility of this particular junction region may play an important role in modulating the association affinity of alpha- and beta-spectrin at the tetramerization site of different isoforms, such as erythroid spectrin and brain spectrin. These findings may provide insight for explaining various physiological and pathological conditions that are a consequence of varying alpha- and beta-subunit self-association affinities in their formation of the various spectrin tetramers.

PubMed: 12672815
DOI: 10.1074/jbc.M300617200

実験手法

SOLUTION NMR