1AJ3

SOLUTION STRUCTURE OF THE SPECTRIN REPEAT, NMR, 20 STRUCTURES

1AJ3 の概要

• エントリーDOI: 10.2210/pdb1aj3/pdb
• 分子名称: ALPHA SPECTRIN (1 entity in total)
• 機能のキーワード: elasticity, membrane skeleton, spectrin, coiled-coil, cytoskeleton, calmodulin-binding, actin-binding, capping protein, calcium-binding, duplication, sh3 domain
• 由来する生物種: Gallus gallus (chicken)
• 細胞内の位置: Cytoplasm, cytoskeleton: P07751
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12828.45

構造登録者

Pascual, J.,Pfuhl, M.,Walther, D.,Saraste, M.,Nilges, M. (登録日: 1997-05-14, 公開日: 1997-07-07, 最終更新日: 2024-05-22)

主引用文献

Pascual, J.,Pfuhl, M.,Walther, D.,Saraste, M.,Nilges, M.
Solution structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coil.
J.Mol.Biol., 273:740-751, 1997

PubMed Abstract: Cytoskeletal proteins belonging to the spectrin family have an elongated structure composed of repetitive units. The three-dimensional solution structure of the 16th repeat from chicken brain alpha-spectrin (R16) has been determined by NMR spectroscopy and distance geometry-simulated annealing calculations. We used a total of 1035 distance restraints, which included 719 NOE-based values obtained by applying the ambiguous restraints for iterative assignment (ARIA) method. In addition, we performed a direct refinement against 1H-chemical shifts. The final ensemble of 20 structures shows an average RMSD of 1.52 A from the mean for the backbone atoms, excluding loops and N and C termini. R16 is made up of three antiparallel alpha-helices separated by two loops, and folds into a left-handed coiled-coil. The basic unit of spectrin is an antiparallel heterodimer composed of two homologous chains, beta and alpha. These assemble a tetramer via a mechanism that relies on the completion of a single repeat by association of the partial repeats located at the C terminus of the beta-chain (two helices) and at the N terminus of the alpha-chain (one helix). This tetramer is the assemblage able to cross-link actin filaments. Model building by homology of the "tetramerization" repeat from human erythrocyte spectrin illuminates the possible role of point mutations which cause hemolytic anemias.

PubMed: 9356261
DOI: 10.1006/jmbi.1997.1344

実験手法

SOLUTION NMR