Accessibility of selenomethionine proteins by total chemical synthesis: structural studies of human herpesvirus‐8 MIP‐II

FEBS Letters

Schweitzer, Barry I¹  Shao, Weiping¹  West, John¹  Lolis, Elias²  Fernandez, Elias²  Thompson, Darren A³  Siani, Michael A³  Wilken, Jill³ 

[1]Walt Disney Memorial Cancer Institute at Florida Hospital, 12722 Research Parkway, Orlando, FL 32826, USA

[2]Department of Pharmacology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06510, USA

[3]Gryphon Sciences, 250 East Grand Avenue, Suite 90, San Francisco, CA 94080, USA

关键词: X-ray crystallography;    Nuclear magnetic resonance;    vMIP-II;    Kaposi sarcoma;    Herpesvirus-8;    Genome;    DQF-COSY;    double quantum filtered correlation spectroscopy;    HSQC;    heteronuclear single quantum coherence;    IL-8;    interleukin-8;    MCP;    monocyte chemoattractant protein;    MIP;    macrophage inflammatory protein;    NMR;    nuclear magnetic resonance;    NOE;    nuclear Overhauser effect;    RANTES;    regulated upon activation;    normal T-cell expressed and presumably secreted;    RMS;    root mean square;    ROESY;    rotating frame Overhauser effect spectroscopy;    [SeMet]-vMIP-II;    selenomethionine-vMIP-II;    TOCSY;    total correlation spectroscopy;   

DOI  :  10.1016/S0014-5793(98)01520-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The determination of high resolution three-dimensional structures by X-ray crystallography or nuclear magnetic resonance (NMR) is a time-consuming process. Here we describe an approach to circumvent the cloning and expression of a recombinant protein as well as screening for heavy atom derivatives. The selenomethionine-modified chemokine macrophage inflammatory protein-II (MIP-II) from human herpesvirus-8 has been produced by total chemical synthesis, crystallized, and characterized by NMR. The protein has a secondary structure typical of other chemokines and forms a monomer in solution. These results indicate that total chemical synthesis can be used to accelerate the determination of three-dimensional structures of new proteins identified in genome programs.

【 授权许可】

Unknown