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. 2014 Aug 29;13:201. doi: 10.1186/1476-4598-13-201

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© El-Baba et al.; licensee BioMed Central Ltd. 2014

This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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TQ binds to PAK1 in the vicinity of Thr212. A. Surface representation of possible active conformation of PAK1 bound to TQ in the vicinity of pPAK1Thr212. TQ is represented in stick (purple). PAK1 residues within the 4 Å interface of the binding site are labelled in red. The kinase domain and the regulatory domain of PAK1 are marked in green and blue respectively. B. Surface representation of the PAK1-ERK2 complex. PAK1 and ERK2 are shown in green and cyan respectively. Position of Thr212 is highlighted in red. C. Surface representation of PAK1-ERK2 complex in the presence of TQ. Positions of Thr212 and TQ are highlighted in red and purple respectively.