ArticleBiophysical journal2000
Is SH1-SH2-cross-linked myosin subfragment 1 a structural analog of the weakly-bound state of myosin?
Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 17 citations in OpenAlex.
- Electrostatic interactions in the force-generating region of the human cardiac myosin modulate ADP dissociation from actomyosin.Biochemical and biophysical research communications · 2019Article
- 3-D structural analysis of the crucial intermediate of skeletal muscle myosin and its role in revised actomyosin cross-bridge cycle.Biophysics (Nagoya-shi, Japan) · 2014Review
- Conformationally trapping the actin-binding cleft of myosin with a bifunctional spin label.The Journal of biological chemistry · 2013Article
- Three distinct actin-attached structural states of myosin in muscle fibers.Biophysical journal · 2012Article
- Structural dynamics of the actomyosin complex probed by a bifunctional spin label that cross-links SH1 and SH2.Biophysical journal · 2008Article
- Nucleotide-induced and actin-induced structural changes in SH1-SH2-modified myosin subfragment 1.Journal of muscle research and cell motility · 2007Article
- Structural characterization of weakly attached cross-bridges in the A*M*ATP state in permeabilized rabbit psoas muscle.Biophysical journal · 2002Article
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2 authors at 1 institution in 1 country.
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Abstract
Myosin subfragment 1 (S1) with SH1 (Cys(707)) and SH2 (Cys(697)) groups cross-linked by p-phenylenedimaleimide (pPDM-S1) is thought to be an analog of the weakly bound states of myosin bound to actin. The structural properties of pPDM-S1 were compared in this study to those of S1.ADP.BeF(x) and S1.ADP.AlF(4)(-), i.e., the established structural analogs of the myosin weakly bound states. To distinguish between the conformational effects of SH1-SH2 cross-linking and those due to their monofunctional modification, we used S1 with the SH1 and SH2 groups labeled with N-phenylmaleimide (NPM-S1) as a control in our experiments. The state of the nucleotide pocket was probed using a hydrophobic fluorescent dye, 3-[4-(3-phenyl-2-pyrazolin-1-yl)benzene-1-sulfonylamido]phen ylboronic acid (PPBA). Differential scanning calorimetry (DSC) was used to study the thermal stability of S1. By both methods the conformational state of pPDM-S1 was different from that of unmodified S1 in the S1.ADP.BeF(x) and S1.ADP.AlF(4)(-) complexes and closer to that of nucleotide-free S1. Moreover, BeF(x) and AlF(4)(-) binding failed to induce conformational changes in pPDM-S1 similar to those observed in unmodified S1. Surprisingly, when pPDM cross-linking was performed on S1.ADP.BeF(x) complex, ADP.BeF(x) protected to some extent the nucleotide pocket of S1 from the effects of pPDM modification. NPM-S1 behaved similarly to pPDM-S1 in our experiments. Overall, this work presents new evidence that the conformational state of pPDM-S1 is different from that of the weakly bound state analogs, S1.ADP.BeF(x) and S1.ADP.AlF(4)(-). The similar structural effects of pPDM cross-linking of SH1 and SH2 groups and their monofunctional labeling with NPM are ascribed to the inhibitory effects of these modifications on the flexibility/mobility of the SH1-SH2 helix.
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