Research article
Molecular basis for defect in Alix-binding by alternatively spliced isoform of ALG-2 (ALG-2ΔGF122) and structural roles of F122 in target recognition
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* Corresponding author: Masatoshi Maki mmaki@agr.nagoya-u.ac.jp
1 Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan
2 Structural Biology Research Center, Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), Tsukuba, Ibaraki 305-0801, Japan
BMC Structural Biology 2010, 10:25 doi:10.1186/1472-6807-10-25
Published: 6 August 2010Additional files
Additional file 1:
Supplementary figures. Showing structures of the calcium-bound dimeric form of des3-23ALG-2ΔGF122 (Figure S1), the metal-free form of des3-20ALG-2 (Figure S2), EF-hand Ca2+-coordination in des3-23ALG-2ΔGF122 (Figure S3), non-canonical Zn2+-coordination in EF5 (Figure S4), and SPR analyses of F122 mutants of ALG-2 for Alix-binding capacities (Figure S5).
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Additional file 2:
Supplementary tables. Showing bond distances for the canonical EF-hand metal ion coordinates in ALG-2 for calcium (Table S1) and zinc (Table S2), bond distance for the non-canonical zinc ion coordinate in EF5 (Table S3), and primers used for site-directed mutagenesis performed in this study (Table S4).
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