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Science 17 October 1986:
Vol. 234. no. 4774, pp. 349 - 352
DOI: 10.1126/science.3489989
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Articles

Science, Vol 234, Issue 4774, 349-352
Copyright © 1986 by American Association for the Advancement of Science

articles

Structure-activity studies of interleukin-2

FE Cohen, PA Kosen, ID Kuntz, LB Epstein, TL Ciardelli, and KA Smith

The critical role of interleukin-2 (IL-2) in immune response heightens the need to know its structure in order to understand its activity. New computer-assisted predictive methods for the assignment of secondary structure together with a method to predict the tertiary structure of a protein from data on its primary sequence and secondary structure were applied to IL-2. This method generated four topological families of structures, of which the most plausible is a right-handed fourfold alpha-helical bundle. Members of this family were shown to be compatible with existing structural data on disulfide bridges and monoclonal antibody binding for IL-2. Experimental estimates of secondary structure from circular dichroism and site-directed mutagenesis data support the model. A region likely to be important in IL-2 binding to its receptor was identified as residues Leu36, Met38, Leu40, Phe42, Phe44, and Met46.


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