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Accessibility of selenomethionine proteins by total chemical synthesis: structural studies of human herpesvirus‐8 MIP‐II
Author(s) -
Shao Weiping,
Fernandez Elias,
Wilken Jill,
Thompson Darren A,
Siani Michael A,
West John,
Lolis Elias,
Schweitzer Barry I
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01520-8
Subject(s) - chemokine , chemistry , selenium , recombinant dna , monomer , cloning (programming) , macrophage inflammatory protein , biochemistry , gene , organic chemistry , polymer , receptor , computer science , programming language
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.