A HYPOTHETICAL STRUCTURAL ROLE FOR PROLINE RESIDUES IN THE FLANKING SEGMENTS OF PROTEIN-PROTEIN INTERACTION SITES

被引:83
作者
KINI, RM [1 ]
EVANS, HJ [1 ]
机构
[1] VIRGINIA COMMONWEALTH UNIV,MED COLL VIRGINIA,DEPT BIOCHEM & MOLEC BIOPHYS,RICHMOND,VA 23298
关键词
D O I
10.1006/bbrc.1995.2084
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
An examination of more than 1600 protein-protein interaction sites indicated that proline is the residue most commonly found near interaction sites. A structural role is distinguished for these proline residues in the flanking segments of protein-protein interaction sites. The unique nature of proline helps protect the integrity and present the sites, thus promoting protein-protein interactions. A novel approach to the design and development of potent peptide drugs and a simple predictive method to identify protein-protein interaction sites directly from the amino acid sequence have been developed based on this finding. The recognition of this structural role for proline has strong implications for protein chemistry and protein engineering. (C) 1995 Academic Press,Inc.
引用
收藏
页码:1115 / 1124
页数:10
相关论文
共 20 条
[1]   ANTIGENIC STRUCTURES OF PROTEINS - THEIR DETERMINATION HAS REVEALED IMPORTANT ASPECTS OF IMMUNE RECOGNITION AND GENERATED STRATEGIES FOR SYNTHETIC MIMICKING OF PROTEIN-BINDING SITES [J].
ATASSI, MZ .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1984, 145 (01) :1-20
[2]  
CARVER JP, 1967, TREATISE COLLAGEN, P441
[3]   NATURE OF ACCESSIBLE AND BURIED SURFACES IN PROTEINS [J].
CHOTHIA, C .
JOURNAL OF MOLECULAR BIOLOGY, 1976, 105 (01) :1-14
[4]  
Chou P Y, 1978, Adv Enzymol Relat Areas Mol Biol, V47, P45
[5]  
CSERZO M, 1989, INT J PEPT PROT RES, V34, P184
[6]  
GONZALEZ FA, 1991, J BIOL CHEM, V266, P22159
[7]  
KINI RM, 1989, INT J PEPT PROT RES, V34, P277
[8]  
KINI RM, 1987, J BIOL CHEM, V262, P14402
[9]  
KINI RM, 1986, TOXICON, V24, P895
[10]  
KINI RM, 1995, UNPUB BIOCH BIOPHYS