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Fig. 6 | Skeletal Muscle

Fig. 6

From: Drosophila myosin mutants model the disparate severity of type 1 and type 2B distal arthrogryposis and indicate an enhanced actin affinity mechanism

Fig. 6

Potential amino acid residue interactions with wild-type residues A234 and F437 as well as with mutant residues A234T and F437I. The Drosophila IFM myosin isoform sequence was modeled onto the scallop muscle myosin II crystal structure in the pre-power stroke state (PDB 1QVI). Switch I is shown in black. Carbon, oxygen, and nitrogen atoms are shown in green, red, and blue, respectively. a Potential hydrophobic interaction between F437 and F245 (located on switch I), with a contact distance of 3.8 Å. b Disruption of the hydrophobic interaction in F437I, with the contact distance extended to 6.8 Å. c Location of A234 in wild type. d Newly formed hydrogen bond interaction between A234T and R273 (not seen in wild type), with a contact distance of 2.7 Å

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Skeletal Muscle

ISSN: 2044-5040

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