摘要
目的研究17个PH结构域中的框架结构。方法利用蛋白质分析软件Clustalx1.83对17个PH结构域的一级结构进行了序列比较,同时也对Loop1,Loop2,Loop3以及β4-β5,β5-β6之间的序列进行比较。根据N-J方法对这17个PH结构域中β1、β2、β3和α螺旋进行聚类分析。结果β1,β2,β3,β4,β5,β6,β7,α螺旋中存在框架结构,分别是K/R-GY/WL-K/RQ,WK/R-RW/YF-L-,I/L-Y/WY/F,GVL/I,X-V/I/T,V/TF-XX,Y/F-F,EE-WI/L-X。结论在这17个PH结构域中存在由保守氨基酸残基构成的框架结构。
Objective To find out the scaffold structure of 17 pleckstrin homology domains. Methods A multiple alignment for the 17 PH domains was built using the Clustalxl. 83 system, and cluster anlysis for 17 β1, β2, β3 strands was carried besded on N-J methods. Results There were scaffolds in 17 PH domains, and they are K/R-GY/W L-K/RQ for β1 , WK/R-RW/YF-L- for β2, I/L - Y/W Y/F for β3, GVL/I for β4, X- -V/I/T for β5, V/TF-XX for β6, Y/F-F for β7, and EE- -WI/L- -X for α helix. Conclusions These scaffolds may provide a framework for PH domain, which may play an important role in the structure of 17 PH domains.
出处
《医学分子生物学杂志》
CAS
CSCD
2007年第2期99-103,共5页
Journal of Medical Molecular Biology