Molecular modeling of the myosin-S1(A1) isoform

Item Type:	Article
Title:	Molecular modeling of the myosin-S1(A1) isoform
Creators Name:	Aydt, E.M. and Wolff, G. and Morano, I.
Abstract:	Type II myosin is the molecular motor which drives contraction upon cyclic interaction with filamentous actin while consuming ATP. The contemporary crystallographic structure of the myosin subfragment-1 (S1) of myosin covers both the motor domain of the heavy chain (MHC) as well as the essential (ELC) and regulatory light chains (RLC). A part of the N-terminus of the ELC is, however, missing in the 3D-models of Type II myosin. The N-terminal domain of the ELC comprises interesting functional features since it binds to actin thus controlling myosin motor activity. For the first time, we modeled the missing 46 N-terminal amino acid of the ELC to the contemporary actin-myosin-S1 complex. We show a rod-like 91A structure being long enough to bridge the gap between the ELC core of myosin-S1 and the appropriate binding site of the ELC on the actin filament.
Keywords:	Myosin, Molecular modeling, 3D-structure, Essential myosin light chain, Animals
Source:	Journal of Structural Biology
ISSN:	1047-8477
Publisher:	Elsevier
Volume:	159
Number:	1
Page Range:	158-163
Date:	July 2007
Official Publication:	https://doi.org/10.1016/j.jsb.2007.04.002
PubMed:	View item in PubMed

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