1b3a: Difference between revisions

==Overview==

BACKGROUND: RANTES is a CC-type chemokine protein that acts as a, chemoattractant for several kinds of leukocytes, playing an important, pro-inflammatory role. Entry of human immunodeficiency virus-1 (HIV-1), into cells depends on the chemokine receptor CCR5. RANTES binds CCR5 and, inhibits HIV-1 entry into peripheral blood cells. Interaction with, chemokine receptors involves a distinct set of residues at the amino, terminus of RANTES. This finding was utilized in the development of a, chemically modified aminooxypentane derivative of RANTES, AOP-RANTES, that, was originally produced from the recombinant protein using semisynthetic, methods. RESULTS: AOP-RANTES has been produced by a novel total chemical, synthesis that provides efficient, direct access to large amounts of this, anti-HIV protein analog. The crystal structure of chemically synthesized, AOP-RANTES has been solved and refined at 1.6 A resolution. The protein is, a dimer, with the amino-terminal pentane oxime moiety clearly defined., CONCLUSIONS: Total chemical synthesis of AOP-RANTES provides a convenient, method of producing the multi-milligram quantities of this protein needed, to investigate the molecular basis of receptor binding and antiviral, activity. This work provides the first truly high-resolution structure of, a RANTES protein, although the structure of RANTES was known from previous, nuclear magnetic resonance (NMR) determinations.

==About this Structure==

[[Category: rantes]]