Leucine is the most stabilizing aliphatic amino acid in the d position of a dimeric leucine zipper coiled coil

被引:119
作者
Moitra, J [1 ]
Szilak, L [1 ]
Krylov, D [1 ]
Vinson, C [1 ]
机构
[1] NCI,BIOCHEM LAB,NIH,BETHESDA,MD 20892
关键词
D O I
10.1021/bi971424h
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The energetic contribution of seven amino acids in the d position of a dimeric leucine zipper coiled coil structure was measured by determining the thermal stability. The d position contains the conserved leucines found in the leucine zipper. We used a natural bZIP protein as our host-guest system that remains dimeric when a single d position is mutated. We have determined the thermal stability, monitored by circular dichroism, of 14 proteins which indicate that alanine is 4.6 kcal mol(-1) per residue less stabilizing than leucine. The similarly sized amino acid isoleucine is 2.9 kcal mol(-1) per residue less stabilizing than leucine, suggesting that leucine is well-packed. Model building indicates that the beta-branched amino acids isoleucine and valine in the d position produced interhelical clashes between the C gamma 2 methyl groups when placed in the favored rotamer conformation. The stabilization by leucine in different d positions is context-dependent; it varies by over 2 kcal mol(-1) in the two positions examined. The order of stabilization is L, M, I, V, C, A, and S. Cysteine in the d position can form a disulfide bond which stabilizes the coiled coil.
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页码:12567 / 12573
页数:7
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