X-RAY STRUCTURES OF ISOFORMS OF THE ACTIN-BINDING PROTEIN PROFILIN THAT DIFFER IN THEIR AFFINITY FOR PHOSPHATIDYLINOSITOL PHOSPHATES

被引：73

作者：

FEDOROV, AA

MAGNUS, KA

GRAUPE, MH

LATTMAN, EE

POLLARD, TD

ALMO, SC

机构：

[1] YESHIVA UNIV ALBERT EINSTEIN COLL MED,DEPT BIOCHEM,BRONX,NY 10461

[2] CASE WESTERN RESERVE UNIV,SCH MED,DEPT BIOCHEM,CLEVELAND,OH 44106

[3] JOHNS HOPKINS UNIV,SCH MED,DEPT BIOPHYS & BIOPHYS CHEM,BALTIMORE,MD 21205

[4] JOHNS HOPKINS UNIV,SCH MED,DEPT CELL BIOL & ANAT,BALTIMORE,MD 21205

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1994年 / 91卷 / 18期

关键词：

D O I：

10.1073/pnas.91.18.8636

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

We determined the structures of Acanthamoeba profilin I and profilin II by x-ray crystallography at resolutions of 2.0 and 2.8 Angstrom, respectively. The polypeptide folds and the actin-binding surfaces of the amoeba profilins are very similar to those of bovine and human profilins. The electrostatic potential surfaces of the two Acanthamoeba isoforms differ. Two areas of high positive potential on the surface of profilin II are candidate binding sites for phosphatidylinositol phosphates. The proximity of these sites to the actin binding site provides an explanation for the competition between actin and lipids for binding profilin.

引用

页码：8636 / 8640

页数：5

共 43 条

[1] THE PRIMARY STRUCTURE OF THE BASIC ISOFORM OF ACANTHAMOEBA PROFILIN [J].