More than Meets the Eye: Hidden Structures in the Proteome

被引:8
|
作者
Wasserman, Hal [1 ]
Saphire, Erica Ollmann [1 ,2 ]
机构
[1] Scripps Res Inst, Dept Immunol & Microbial Sci, La Jolla, CA 92037 USA
[2] Scripps Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA
来源
关键词
transformer; metamorphic protein; morpheein; moonlighting protein; matrix; Ebola virus; INFLUENZA-A-VIRUS; HEPATITIS-B-VIRUS; LYMPHOCYTIC CHORIOMENINGITIS VIRUS; NS1 EFFECTOR DOMAIN; X-RAY-STRUCTURE; EBOLA-VIRUS; MATRIX PROTEIN; CRYSTAL-STRUCTURE; SV40-TRANSFORMED CELLS; BINDING-PROPERTIES;
D O I
10.1146/annurev-virology-100114-054923
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
A central dogma of molecular biology is that the sequence of a protein dictates its particular fold and the fold dictates its function. Indeed, the sequence. structure. function hypothesis has been a guiding principle by which scientists approach molecular biology. Every student knows that the genome encodes information for the progression from primary sequence to secondary, tertiary, and ultimately quaternary structure. Yet with a growing number of proteins, a fifth level has been identified: rearrangement of existing structures into distinct forms. Recent observations indicate that replication of Ebola virus depends on this fifth level. We believe other viruses with compact genomes and rapid evolution under selective pressure will be a rich source of examples of polypeptides that rearrange to gain added functions. In this review, we describe mechanisms by which viral, prokaryotic, and eukaryotic polypeptides have adopted alternate structures to control or gain function.
引用
收藏
页码:373 / 386
页数:14
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