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. 2017 Jul 7;9(1-2):22–48. doi: 10.1080/21541248.2017.1336191

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© 2017 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.

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Figure 4. — Rab partner recognition sites. Rab (Rab3a, 3RAB) Mg²⁺-GTP (dark gray) bound structure with the structural elements contributing to partner binding highlighted. (A) Side view showing the Rab canonical effector binding site composed of Switch1, Interswitch, and Switch2; surrounded by complementarity determining regions (CDR1–5, shown in orange). Conserved Rab hydrophobic triad is shown in yellow sticks. The surface representation is shown in the middle, and conservation of surface residues (based on the sequence alignment in Fig. 1) generated using ConSurf web server ¹⁵⁰ is presented on the right. (B) Top view showing a new, secondary Rab effector binding site composed of the CDR4 and CDR5 regions flanking the nucleotide binding pocket.