1AEY

ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, SOLUTION NMR, 15 STRUCTURES

1AEY の概要

• エントリーDOI: 10.2210/pdb1aey/pdb
• 分子名称: ALPHA-SPECTRIN (1 entity in total)
• 機能のキーワード: cytoskeleton, 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: 7229.24

構造登録者

Blanco, F.J.,Ortiz, A.R.,Serrano, L. (登録日: 1997-03-02, 公開日: 1997-05-15, 最終更新日: 2024-05-22)

主引用文献

Blanco, F.J.,Ortiz, A.R.,Serrano, L.
1H and 15N NMR assignment and solution structure of the SH3 domain of spectrin: comparison of unrefined and refined structure sets with the crystal structure.
J.Biomol.NMR, 9:347-357, 1997

PubMed Abstract: The assignment of the 1H and 15N nuclear magnetic resonance spectra of the Src-homology region 3 domain of chicken brain alpha-spectrin has been obtained. A set of solution structures has been determined from distance and dihedral angle restraints, which provide a reasonable representation of the protein structure in solution, as evaluated by a principal component analysis of the global pairwise root-mean-square deviation (rmsd) in a large set of structures consisting of the refined and unrefined solution structures and the crystal structure. The solution structure is well defined, with a lower degree of convergence between the structures in the loop regions than in the secondary structure elements. The average pairwise rmsd between the 15 refined solution structures is 0.71 +/- 0.13 A for the backbone atoms and 1.43 +/- 0.14 A for all heavy atoms. The solution structure is basically the same as the crystal structure. The average rmsd between the 15 refined solution structures and the crystal structure is 0.76 A for the backbone atoms and 1.45 +/- 0.09 A for all heavy atoms. There are, however, small differences probably caused by intermolecular contacts in the crystal structure.

PubMed: 9255941
DOI: 10.1023/A:1018330122908

実験手法

SOLUTION NMR