A molecular model of a point mutation (Val297Met) in the serine protease domain of protein C
A molecular model of a point mutation (Val297Met) in the serine protease domain of protein C
复制标题
蛋白 C 丝氨酸蛋白酶结构域点突变 (Val297Met) 的分子模型
DOI：
10.1038/emm.1999.8
复制
发表时间：
1999
影响因子：
12.8
通讯作者：
Q. Park
中科院分区：
文献类型：
--
作者：
K. Song;Y. Park;J. Choi;H. K. Kim;Q. Park
A heterozygous GTG to ATG (Val297Met) mutation was detected in a patient with inherited protein C deficiency and deep vein thrombosis. Cosegregation of the mutation with protein C deficiency was observed through a family pedigree study. Molecular models of the serine protease domains of wild type and mutant protein C were constructed by standard comparative method. Val 297 was found to be located in the hydrophobic core of the protein. Although the substitution of Met for Val does not greatly alter the hydrophobicity of the protein, it introduces a bulkier side chain, which yields steric hindrance between this residue and adjacent residues, such as Met364, Tyr393, Ile321, Ile323, and Val378. It seems that the Met can not fit into the tight packing into which it is trapped, thereby probably inducing misfolding and/or greater instability of the protein. Such misfolding and/or instability thereby eventually disturbs the catalytic triad, in consistent with the observed type I deficiency state.
人类蛋白 C 基因的进化和组织。
DOI：
10.1073/pnas.83.3.546
发表时间：
1986
影响因子：
11.1
作者：
Plutzky,J;Hoskins,JA;Long,GL;Crabtree,GR
通讯作者：
Crabtree,GR
DOI：
10.1073/pnas.81.15.4766
发表时间：
1984-01-01
期刊：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES
影响因子：
--
作者：
FOSTER, D;DAVIE, EW
通讯作者：
DAVIE, EW