The solution NMR structure of a blue-green algae hepatotoxin, microcystin-RR - A comparison with the structure of microcystin-LR

被引：14

作者：

Trogen, GB

Edlund, U

Larsson, G

Sethson, I ^{[1
]}

机构：

[1] Umea Univ, Dept Organ Chem, S-90187 Umea, Sweden

[2] Umea Univ, Dept Med Biochem & Biophys, S-90187 Umea, Sweden

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1998年 / 258卷 / 02期

关键词：

microcystins; cyanobacteria; protein phosphatase; three-dimensional structure; simulated annealing;

D O I：

10.1046/j.1432-1327.1998.2580301.x

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 microcystin-RR structures are compared with the structures of microcystin-LR in solution as well as in the crystal structure of the complex with protein phosphatase. The gross structures of the two peptides are similar, but with a more accentuated and compact saddle structure for microcystin-RR. The structural differences affect the hydrogen-bond pattern in the peptides and the location of the side chain of N-methyldehydroalanine, both of which are important for the ability of the peptide to form a tight complex with protein phosphatase. These structural differences may contribute to the observed differences in toxicity of microcystin-RR and microcystin-LR.

引用

页码：301 / 312

页数：12

共 55 条

[1] Solution structure of nodularin - An inhibitor of serine/threonine-specific protein phosphatases [J].