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. 2012 May 4;7(5):e36526. doi: 10.1371/journal.pone.0036526

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Anand et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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(A) The different ligands (sulfate (violet), phosphoserine (salmon), Ins(4)P (green) and also the turned-over Ins(4)P (light blue)) are occupying the same non-canonical binding pocket, confirming the readily available large binding site of the Slm1-PH. (B) Stereo diagram of PtdIns(4,5)P₂ (atom colors) modeled in the non-canonical binding site of Slm1-PH (green) and overlaid onto the β-spectrin PH domain (wheat color). This shows the conservation of side chains that contact the ligands.