Accessibility of selenomethionine proteins by total chemical synthesis: structural studies of human herpesvirus-8 MIP-II.
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.
Shao
W
W
Walt Disney Memorial Cancer Institute at Florida Hospital, Orlando 32826, USA.
Fernandez
E
E
Wilken
J
J
Thompson
D A
DA
Siani
M A
MA
West
J
J
Lolis
E
E
Schweitzer
B I
BI
D000595:Amino Acid Sequence; D054426:Chemokine CXCL2; D002630:Chemotactic Factors / Q000737:chemistry*; D018360:Crystallography, X-Ray; D019288:Herpesvirus 8, Human; D006801:Humans; D008969:Molecular Sequence Data; D015846:Monokines / Q000138:chemical synthesis / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D012645:Selenomethionine; D012996:Solutions
D054426:Chemokine CXCL2; D002630:Chemotactic Factors; D015846:Monokines; D012996:Solutions; D012645:Selenomethionine