Conformational dimorphism and transmembrane orientation of prion protein residues 110-136 in bicelles

被引：38

作者：

Glover, KJ ^{[1
]}

Whiles, JA ^{[1
]}

Wood, MJ ^{[1
]}

Melacini, G ^{[1
]}

Komives, EA ^{[1
]}

Vold, RR ^{[1
]}

机构：

[1] Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA

来源：

BIOCHEMISTRY | 2001年 / 40卷 / 44期

关键词：

D O I：

10.1021/bi011485m

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：

A fragment corresponding to the putative membrane-associating domain of the prion protein (residues 110-136) was analyzed in phospholipid bicelles. Prion(110-136) associated with bicelles and exhibited a lipid- and pH-dependent conformational dimorphism between unstructured (pH 4.5) and a-helical (pH 7.5). Mutational analysis indicated that the charge state of a single histidine residue was largely responsible for the dimorphism. Amide-lipid NOEs and amide-water chemical exchange measurements revealed that the helical conformation of prion(110-136) spanned the bilayer, and were corroborated by solid-state deuterium NMR experiments indicating that the helical axis rested at a 16 degrees angle with respect to the bilayer normal.

引用

页码：13137 / 13142

页数：6

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