THE CONFORMATION OF A-FACTOR IS NOT INFLUENCED BY THE S-PRENYLATION OF CYS12

被引：11

作者：

GOUNARIDES, JS

BROIDO, MS

XUE, CB

BECKER, JM

NAIDER, FR

机构：

[1] CUNY,GRAD SCH,STATEN ISL,NY 10301

[2] CUNY COLL STATEN ISL,STATEN ISL,NY 10301

[3] CUNY,GRAD SCH,NEW YORK,NY 10021

[4] UNIV TENNESSEE,DEPT MICROBIOL,KNOXVILLE,TN 37996

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 181卷 / 03期

关键词：

D O I：

10.1016/0006-291X(91)92055-O

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：

Two-Dimensional NMR was used to examine the solution conformation of the lipopeptide a-factor, YIIKGVFWDPAC(S-farnesyl) OCH3, from the yeast Saccharomyces cerevisiae and five analogues containing various S-alkylated cysteines in DMSO-d6. NOESY data, NH temperature coefficients, and 3JαNH coupling constants indicate that the a-factor is a predominantly unstructured peptide in DMSO. Similar results were obtained for the other peptides indicating that S-prenylation of Cys12 does not affect the conformation of these peptides. © 1991.

引用

页码：1125 / 1130

页数：6

共 19 条

[1]

ANDEREGG RJ, 1988, J BIOL CHEM, V263, P18236

[2]

BALARAM P, 1985, P INDIAN AS-CHEM SCI, V95, P21

[3] A-FACTOR FROM SACCHAROMYCES-CEREVISIAE - PARTIAL CHARACTERIZATION OF A MATING HORMONE PRODUCED BY CELLS OF MATING TYPE-A [J].