The crystal structure of Met-RANTES: Comparison with native RANTES and AOP-RANTES

David M. Hoover, Jeffrey Shaw, Zygmunt Gryczynski, Amanda E.I. Proudfoot, Tim Wells, Jacek Lubkowski

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

Met-RANTES is a modified version of the chemokine RANTES, which has an additional amino acid at the amino terminus. To compare Met-RANTES with the native protein as well as with another antagonist, AOP-RANTES, we have solved the structure of Met-RANTES at 1.6 Å by X-ray crystallography and investigated the dimerization of all three proteins by fluorescence anisotropy. The dimerization of AOP-RANTES shows an altered aggregation profile. The delineation of slight differences in binding sulfate anions by Met- and AOP-RANTES might be linked to specific yet different interactions between these proteins and glycosaminoglycans.

Original languageEnglish
Pages (from-to)73-82
Number of pages10
JournalProtein and Peptide Letters
Volume7
Issue number2
StatePublished - 1 Dec 2000

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    Hoover, D. M., Shaw, J., Gryczynski, Z., Proudfoot, A. E. I., Wells, T., & Lubkowski, J. (2000). The crystal structure of Met-RANTES: Comparison with native RANTES and AOP-RANTES. Protein and Peptide Letters, 7(2), 73-82.