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. 2017 Apr 1;18(4):748. doi: 10.3390/ijms18040748

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© 2017 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Characterization of the CXCL7-CXCL1 trapped heterodimer. (A) Trapping strategy showing cysteine mutations (in red) that will result only in a trapped heterodimer. Cysteines are too far away in the homodimer for disulfide formation; (B) A schematic of the heterodimer showing the location of the disulfide across the heterodimer interface and away from the two fold symmetry axis. CXCL7 is in cyan and CXCL1 is in green. (C) SDS-PAGE gel showing the formation of the disulfide bond. The higher molecular weight heterodimer band is observed only under non-reducing conditions. BME stands for β-mercaptoethanol.