1BK2

A-SPECTRIN SH3 DOMAIN D48G MUTANT

1BK2 の概要

• エントリーDOI: 10.2210/pdb1bk2/pdb
• 分子名称: A-SPECTRIN (2 entities in total)
• 機能のキーワード: sh3-domain, cytoskeleton, calmodulin-binding, actin-binding
• 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: 6637.66

構造登録者

Martinez, J.C.,Pisabarro, M.T.,Serrano, L. (登録日: 1998-07-14, 公開日: 1999-02-16, 最終更新日: 2024-05-22)

主引用文献

Martinez, J.C.,Pisabarro, M.T.,Serrano, L.
Obligatory steps in protein folding and the conformational diversity of the transition state.
Nat.Struct.Biol., 5:721-729, 1998

PubMed Abstract: We have analyzed the existence of obligatory steps in the folding reaction of the alpha-spectrin SH3 domain by mutating Asp 48 (D48G), which is at position i+3 of an isolated two-residue type II' beta-turn. Calorimetry and X-ray analysis show an entropic stabilizing effect resulting from local changes at the dihedral angles of the beta-turn. Kinetic analysis of D48G shows that this beta-turn is fully formed in the transition state, while there is no evidence of its formation in an isolated fragment. Introduction of several mutations in the D48G protein reveals that the local stabilization has not significantly altered the transition state ensemble. All these results, together with previous analysis of other alpha-spectrin and src SH3 mutants, indicate that: (i) in the folding reaction there could be obligatory steps which are not necessarily part of the folding nucleus; (ii) transition state ensembles in beta-sheet proteins could be quite defined and conformationally restricted ('mechanic folding nucleus'); and (iii) transition state ensembles in some proteins could be evolutionarily conserved.

PubMed: 9699637
DOI: 10.1038/1418

実験手法

X-RAY DIFFRACTION (2.01 Å)