RULES FOR ALPHA-HELIX TERMINATION BY GLYCINE

被引:276
作者
AURORA, R [1 ]
SRINIVASAN, R [1 ]
ROSE, GD [1 ]
机构
[1] WASHINGTON UNIV, SCH MED, DEPT BIOCHEM & MOLEC BIOPHYS, ST LOUIS, MO 63110 USA
关键词
D O I
10.1126/science.8178170
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
A predictive rule for protein folding is presented that involves two recurrent glycine-based motifs that cap the carboxyl termini of cr. helices. In proteins, helices that terminated in glycine residues were found predominantly in one of these two motifs. These glycine structures had a characteristic pattern of polar and apolar residues. Visual inspection of known helical sequences was sufficient to distinguish the two motifs from each other and from internal glycines that fail to terminate helices. These glycine motifs-in which the local sequence selects between available structures-represent an example of a stereochemical rule for protein folding.
引用
收藏
页码:1126 / 1130
页数:5
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[1]   CONTRIBUTIONS OF HYDROGEN-BONDS OF THR-157 TO THE THERMODYNAMIC STABILITY OF PHAGE-T4 LYSOZYME [J].
ALBER, T ;
SUN, DP ;
WILSON, K ;
WOZNIAK, JA ;
COOK, SP ;
MATTHEWS, BW .
NATURE, 1987, 330 (6143) :41-46
[2]   PRINCIPLES THAT GOVERN FOLDING OF PROTEIN CHAINS [J].
ANFINSEN, CB .
SCIENCE, 1973, 181 (4096) :223-230
[3]   HYDROGEN-BONDING IN GLOBULAR-PROTEINS [J].
BAKER, EN ;
HUBBARD, RE .
PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY, 1984, 44 (02) :97-179
[4]   DISSECTION OF HELIX CAPPING IN T4 LYSOZYME BY STRUCTURAL AND THERMODYNAMIC ANALYSIS OF 6 AMINO-ACID SUBSTITUTIONS AT THR 59 [J].
BELL, JA ;
BECKTEL, WJ ;
SAUER, U ;
BAASE, WA ;
MATTHEWS, BW .
BIOCHEMISTRY, 1992, 31 (14) :3590-3596
[5]   PROTEIN DATA BANK - COMPUTER-BASED ARCHIVAL FILE FOR MACROMOLECULAR STRUCTURES [J].
BERNSTEIN, FC ;
KOETZLE, TF ;
WILLIAMS, GJB ;
MEYER, EF ;
BRICE, MD ;
RODGERS, JR ;
KENNARD, O ;
SHIMANOUCHI, T ;
TASUMI, M .
JOURNAL OF MOLECULAR BIOLOGY, 1977, 112 (03) :535-542
[6]   ON ALPHA-HELICES TERMINATED BY GLYCINE .2. RECOGNITION BY SEQUENCE PATTERNS [J].
BORK, P ;
PREISSNER, R .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1991, 180 (02) :666-672
[7]   SIDE CHAIN-BACKBONE HYDROGEN-BONDING CONTRIBUTES TO HELIX STABILITY IN PEPTIDES DERIVED FROM AN ALPHA-HELICAL REGION OF CARBOXYPEPTIDASE-A [J].
BRUCH, MD ;
DHINGRA, MM ;
GIERASCH, LM .
PROTEINS-STRUCTURE FUNCTION AND GENETICS, 1991, 10 (02) :130-139
[8]   HELIX CAPPING PROPENSITIES IN PEPTIDES PARALLEL THOSE IN PROTEINS [J].
CHAKRABARTTY, A ;
DOIG, AJ ;
BALDWIN, RL .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (23) :11332-11336
[9]  
COCCO MJ, IN PRESS PROTEIN SCI
[10]   SIDE-CHAIN ENTROPY OPPOSES ALPHA-HELIX FORMATION BUT RATIONALIZES EXPERIMENTALLY DETERMINED HELIX-FORMING PROPENSITIES [J].
CREAMER, TP ;
ROSE, GD .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1992, 89 (13) :5937-5941