2OAW

Structure of SHH variant of "Bergerac" chimera of spectrin SH3

2OAW の概要

• エントリーDOI: 10.2210/pdb2oaw/pdb
• 関連するPDBエントリー: 1BK2 1SHG
• 分子名称: Spectrin alpha chain, brain, CHLORIDE ION (3 entities in total)
• 機能のキーワード: sh3 domain, chimera, structural protein
• 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: 4
• 化学式量合計: 30730.28

構造登録者

Gabdoulkhakov, A.G.,Gushchina, L.V.,Nikulin, A.D.,Nikonov, S.V.,Viguera, A.R.,Serrano, L.,Filimonov, V.V. (登録日: 2006-12-18, 公開日: 2008-04-08, 最終更新日: 2023-08-30)

主引用文献

Gushchina, L.V.,Gabdulkhakov, A.G.,Nikonov, S.V.,Mateo, P.L.,Filimonov, V.V.
Structural and thermodynamic studies of Bergerac-SH3 chimeras.
Biophys.Chem., 139:106-115, 2009

PubMed Abstract: Bergerac-type chimeras of spectrin SH3 were designed by extending a beta-hairpin by eight amino acids so that the extension protruded from the domain body like a "nose" being exposed to the solvent. A calorimetric study of several Bergerac-SH3 variants was carried out over a wide range of pH values and protein concentrations and the three-dimensional structure of one of them, SHH, was determined. X-ray studies confirmed that the nose had a well defined beta-structure whilst the chimera formed a stable tetramer within the crystal unit because of four tightly packed noses. In the pH range of 4-7 the heat-induced unfolding of some chimeras was complex and concentration dependent, whilst at pH values below 3.5, low protein concentrations of all the chimeras studied, including SHH, seemed to obey a monomolecular two-state unfolding model. The best set of data was obtained for the SHA variant, the unfolding heat effects of which were systematically higher than those of the WT protein (about 16.4 kJ/mol at 323 K), which may be close to the upper limit of the enthalpy gain due to 10 residue beta-hairpin folding. At the same time, the chimeras with high nose stability, which, like SHH, have a hydrophobic (IVY) cluster on their surface, showed a lower apparent unfolding heat effect, much closer to that of the WT protein. The possible reasons for this difference are discussed.

PubMed: 19042078
DOI: 10.1016/j.bpc.2008.10.011

実験手法

X-RAY DIFFRACTION (1.9 Å)