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

被引：14

作者：

Shao, WP

Fernandez, E

Wilken, J

Thompson, DA

Siani, MA

West, J

Lolis, E

Schweitzer, BI

机构：

[1] Yale Univ, Sch Med, Dept Pharmacol, New Haven, CT 06510 USA

[2] Florida Hosp, Walt Disney Mem Canc Inst, Orlando, FL 32826 USA

[3] Gryphon Sci, San Francisco, CA 94080 USA

来源：

FEBS LETTERS | 1998年 / 441卷 / 01期

关键词：

X-ray crystallography; nuclear magnetic resonance; vMIP-II; Kaposi sarcoma; herpesvirus-8; genome;

D O I：

10.1016/S0014-5793(98)01520-8

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 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 herpes-virus-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. (C) 1998 Federation of European Biochemical Societies.

引用

页码：77 / 82

页数：6

共 29 条

[1] ASSOCIATION OF BIOMOLECULAR SYSTEMS VIA PULSED-FIELD GRADIENT NMR SELF-DIFFUSION MEASUREMENTS [J].