Key result
Crystal structures of Myo2-GTD in complex with cargo adaptors Smy1, Inp2, and Mmr1 revealed a highly flexible hydrophobic groove in subdomain-I that accommodates diverse protein sequences.
Why the study?
Little is known about the capacity of the yeast class V myosin Myo2-GTD to recognize a diverse array of cargos specifically at the molecular level.
Structural analysis of yeast Myo2-GTD reveals a flexible hydrophobic groove that explains its ability to recognize diverse cellular cargos.
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No immediate clinical implications for cardiovascular care; leaves open extensions to myosin roles in cardiac transport.
Tang et al. (2019) studied this question. Crystal structures of Myo2-GTD in complex with cargo adaptor proteins was evaluated on Crystal structures of Myo2-GTD at 1.9-3.1 Å resolutions. Crystal structures of Myo2-GTD in complex with cargo adaptors Smy1, Inp2, and Mmr1 revealed a highly flexible hydrophobic groove in subdomain-I that accommodates diverse protein sequences.
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