Polyproline-II Helix in Proteins: Structure and Function

被引:439
作者
Adzhubei, Alexei A. [1 ]
Sternberg, Michael J. E. [2 ]
Makarov, Alexander A. [1 ]
机构
[1] Russian Acad Sci, Engelhard Inst Mol Biol, Moscow 119991, Russia
[2] Univ London Imperial Coll Sci Technol & Med, Div Mol Biosci, Struct Bioinformat Grp, London SW7 2AX, England
基金
英国生物技术与生命科学研究理事会;
关键词
PPII conformation; extended left-handed helix; secondary structure; protein interactions; folded and unfolded proteins; RAMAN OPTICAL-ACTIVITY; POLY-L-PROLINE; INTRINSICALLY DISORDERED PROTEIN; MOLECULAR-DYNAMICS SIMULATIONS; ELECTRONIC CIRCULAR-DICHROISM; RANDOM-COIL BEHAVIOR; SRC FAMILY KINASES; SECONDARY STRUCTURE; CRYSTAL-STRUCTURE; PRION PROTEIN;
D O I
10.1016/j.jmb.2013.03.018
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
The poly-L-proline type II (PPII) helix in recent years has emerged clearly as a structural class not only of fibrillar proteins (in collagen, PPII is a dominant conformation) but also of the folded and unfolded proteins. Although much less abundant in folded proteins than the alpha-helix and beta-structure, the left-handed, extended PPII helix represents the only frequently occurring regular structure apart from these two structure classes. Natively unfolded proteins have a high content of the PPII helices identified by spectroscopic methods. Apart from the structural function, PPII is favorable for protein-protein and protein-nucleic acid interactions and plays a major role in signal transduction and protein complex assembly, as this structure is often found in binding sites, specifically binding sites of widely spread SH3 domains. PPII helices do not necessarily contain proline, but proline has high PPII propensity. Commonly occurring proline-rich regions, serving as recognition sites, are likely to have PPII structure. PPII helices are involved in transcription, cell motility, self-assembly, elasticity, and bacterial and viral pathogenesis, and has an important structural role in amyloidogenic proteins. However, PPII helices are not always assigned in experimentally solved structures, and they are rarely used in protein structure modeling. We aim to give an overview of this structural class and of the place it holds in our current understanding of protein structure and function. This review is subdivided into three main parts: the first part covers PPII helices in unfolded peptides and proteins, the second part includes studies of the PPII helices in folded proteins, and the third part discusses the functional role of the PPII. (c) 2013 Elsevier Ltd. All rights reserved.
引用
收藏
页码:2100 / 2132
页数:33
相关论文
共 224 条
[1]   CONSERVATION OF POLYPROLINE-II HELICES IN HOMOLOGOUS PROTEINS - IMPLICATIONS FOR STRUCTURE PREDICTION BY MODEL-BUILDING [J].
ADZHUBEI, AA ;
STERNBERG, MJE .
PROTEIN SCIENCE, 1994, 3 (12) :2395-2410
[2]   APPROACHING A COMPLETE CLASSIFICATION OF PROTEIN SECONDARY STRUCTURE [J].
ADZHUBEI, AA ;
EISENMENGER, F ;
TUMANYAN, VG ;
ZINKE, M ;
BRODZINSKI, S ;
ESIPOVA, NG .
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS, 1987, 5 (03) :689-704
[3]   LEFT-HANDED POLYPROLINE-II HELICES COMMONLY OCCUR IN GLOBULAR-PROTEINS [J].
ADZHUBEI, AA ;
STERNBERG, MJE .
JOURNAL OF MOLECULAR BIOLOGY, 1993, 229 (02) :472-493
[4]   3RD TYPE OF SECONDARY STRUCTURE - NONCOOPERATIVE MOBILE CONFORMATION - PROTEIN DATA-BANK ANALYSIS [J].
ADZHUBEI, AA ;
EISENMENGER, F ;
TUMANYAN, VG ;
ZINKE, M ;
BRODZINSKI, S ;
ESIPOVA, NG .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1987, 146 (03) :934-938
[5]   The prion's elusive reason for being [J].
Aguzzi, Adriano ;
Baumann, Frank ;
Bremer, Jullane .
ANNUAL REVIEW OF NEUROSCIENCE, 2008, 31 :439-477
[6]   Mechanism of fast peptide recognition by SH3 domains [J].
Ahmad, Mazen ;
Gu, Wei ;
Helms, Volkhard .
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2008, 47 (40) :7626-7630
[7]   Crystal Structure of the Src Family Kinase Hck SH3-SH2 Linker Regulatory Region Supports an SH3-dominant Activation Mechanism [J].
Alvarado, John J. ;
Betts, Laurie ;
Moroco, Jamie A. ;
Smithgall, Thomas E. ;
Yeh, Joanne I. .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2010, 285 (46) :35455-35461
[8]   STRUCTURE OF POLY-L-PROLINE 2 [J].
ARNOTT, S ;
DOVER, SD .
ACTA CRYSTALLOGRAPHICA SECTION B-STRUCTURAL CRYSTALLOGRAPHY AND CRYSTAL CHEMISTRY, 1968, B 24 :599-&
[9]   The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling [J].
Arold, S ;
Franken, P ;
Strub, MP ;
Hoh, F ;
Benichou, S ;
Benarous, R ;
Dumas, C .
STRUCTURE, 1997, 5 (10) :1361-1372
[10]   UV Raman demonstrates that α-helical polyalanine peptides melt to polyproline II conformations [J].
Asher, SA ;
Mikhonin, AV ;
Bykov, S .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2004, 126 (27) :8433-8440