Interfacial metal coordination in engineered protein and peptide assemblies

被引:73
|
作者
Sontz, Pamela A. [1 ]
Song, Woon Ju [1 ]
Tezcan, F. Akif [1 ]
机构
[1] Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA
基金
美国国家科学基金会;
关键词
COILED-COIL PEPTIDE; STRUCTURAL-CHARACTERIZATION; SYNTHETIC BIOLOGY; FERRITIN CAGE; APO-FERRITIN; DESIGN; ION; CHEMISTRY; OLIGOMERIZATION; METALLOPROTEINS;
D O I
10.1016/j.cbpa.2013.12.013
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
Metal ions are frequently found in natural protein-protein interfaces, where they stabilize quaternary or supramolecular protein structures, mediate transient protein-protein interactions, and serve as catalytic centers. Paralleling these natural roles, coordination chemistry of metal ions is being increasingly utilized in creative ways toward engineering and controlling the assembly of functional supramolecular peptide and protein architectures. Here we provide a brief overview of this emerging branch of metalloprotein/peptide engineering and highlight a few select examples from the recent literature that best capture the diversity and future potential of approaches that are being developed.
引用
收藏
页码:42 / 49
页数:8
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