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Protein Science (2004), 13:2022-2028. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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NMR structure of CXCR3 binding chemokine CXCL11 (ITAC)

Valerie Booth1,3, Ian Clark-Lewis2,4 and Brian D. Sykes1

1 Protein Engineering Network of Centres of Excellence (PENCE) and University of Alberta, Edmonton, Alberta, T5G 2S2, Canada
2 University of British Columbia, Biomedical Research Centre and Department of Biochemistry and Molecular Biology, Vancouver, British Columbia, V6T 1Z3, Canada

(RECEIVED April 5, 2004; FINAL REVISION May 13, 2004; ACCEPTED May 14, 2004)

CXCL11 (ITAC) is one of three chemokines known to bind the receptor CXCR3, the two others being CXCL9 (Mig) and CXCL10 (IP-10). CXCL11 differs from the other CXCR3 ligands in both the strength and the particularities of its receptor interactions: It has a higher affinity, is a stronger agonist, and behaves differently when critical N-terminal residues are deleted. The structure of CXCL11 was determined using solution NMR to allow comparison with that of CXCL10 and help elucidate the source of the differences. CXCL11 takes on the canonical chemokine fold but exhibits greater conformational flexibility than has been observed for related chemokines under the same sample conditions. Unlike related chemokines such as IP-10 and IL-8, ITAC does not appear to form dimers at millimolar concentrations. The origin for this behavior can be found in the solution structure, which indicates a {beta}-bulge in {beta}-strand 1 that distorts the dimerization interface used by other CXC chemokines.

Keywords: ITAC; CXCL11; structure; NMR; chemokine

Reprint requests to: Brian D. Sykes, University of Alberta, 713 HMRC, Edmonton, AB, T5G 2S2, Canada; e-mail: brian.sykes{at}ualberta.ca; fax: (780) 492-0886.

3 Present address: Department of Biochemistry, Memorial University of Newfoundland, St. John’s, NL, A1B 3X7, Canada.

4 Deceased.

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.04791404.


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