Structural insights into the interaction between a potent anti-inflammatory protein, viral CC chemokine inhibitor (vCCI), and the human CC chemokine, eotaxin-1

Nai Wei Kuo, Yong Guang Gao, Megan S. Schill, Nancy Isern, Cynthia M. Dupureur, Patricia J. Li Wang

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

Background: The mechanism used by viral protein vCCI to tightly bind to many CC chemokines is not known. Results: Specific positively charged residues in the chemokine eotaxin-1 mediate binding to vCCI. Conclusion: Basic residues in the chemokine each provide incremental affinity for vCCI. Significance: This work shows how vCCI can bind a variety of CC chemokines.

Original languageEnglish (US)
Pages (from-to)6592-6603
Number of pages12
JournalJournal of Biological Chemistry
Volume289
Issue number10
DOIs
StatePublished - Mar 7 2014
Externally publishedYes

Fingerprint Dive into the research topics of 'Structural insights into the interaction between a potent anti-inflammatory protein, viral CC chemokine inhibitor (vCCI), and the human CC chemokine, eotaxin-1'. Together they form a unique fingerprint.

  • Cite this