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          Institute: MPI für medizinische Forschung     Collection: Protein - Kristallographie XDS     Display Documents

ID: 565769.0, MPI für medizinische Forschung / Protein - Kristallographie XDS
Curvature variation along the tropomyosin molecule
Translation of Title:Curvature variation along the tropomyosin molecule
Authors:Li, Xiaochuan Edward; Lehman, William; Fischer, Stefan; Holmes, Kenneth C.
Date of Publication (YYYY-MM-DD):2010-05-01
Title of Journal:Journal of Structural Biology
Journal Abbrev.:J. Struct. Biol.
Issue / Number:2
Start Page:307
End Page:312
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description:Complementarity between the tropomyosin supercoil and the helical contour of actin−filaments is
required for the binding interaction of actin and tropomyosin (Li et al., 2010). Clusters of small alanine
residues in place of canonical leucines along coiled−coil tropomyosin may be responsible for pre−shaping
tropomyosin and promoting conformational complementarity to F−actin. A longitudinal displacement
between the two chains of the tropomyosin coiled−coil induced by the alanine clusters could produce
localized bending or limited flexibility along tropomyosin needed to shape tropomyosin (Brown and
Cohen, 2005). To evaluate the influence of alanine clusters on tropomyosin curvature, we calculated
the longitudinal displacement between amino acid residues on adjacent chains of the tropomyosin
coiled−coil and related this ‘‘Z−displacement" to the position of the alanine clusters. Measurements were
made on high−resolution crystal structures of tropomyosin fragments and on trajectories from molecular
dynamics simulations of full−length aa−tropomyosin. We found no strict one−for−one spatial correlation
between alanine cluster position and the Z−displacement. Neither did we find any direct correspondence
between the clusters and the local curvature of tropomyosin. Rather than just causing specific local structural
effects, the overall influence of alanine clusters is complex and delocalized, leading to a gradually
changing bending pattern along the length of tropomyosin
Last Change of the Resource (YYYY-MM-DD):--
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biophysik/Protein - Kristallographie XDS
MPI für medizinische Forschung/Abteilung Biophysik/Muskelforschung
MPI für medizinische Forschung/Abteilung Biophysik
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