English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Curvature variation along the tropomyosin molecule

Li, X. E., Lehman, W., Fischer, S., & Holmes, K. C. (2010). Curvature variation along the tropomyosin molecule. Journal of Structural Biology, 170(2), 307-312. doi:10.1016/j.jsb.2009.12.017.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-8075-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-8076-1
Genre: Journal Article
Alternative Title : Curvature variation along the tropomyosin molecule

Files

show Files
hide Files
:
JStructChem_170_2010_307.pdf (Any fulltext), 953KB
 
File Permalink:
-
Name:
JStructChem_170_2010_307.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, Heidelberg; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Creators

show
hide
 Creators:
Li, Xiaochuan Edward, Author
Lehman, William, Author
Fischer, Stefan, Author
Holmes, Kenneth C.1, Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

Content

show
hide
Free keywords: -
 Abstract: 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 alphaalpha-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.

Details

show
hide
Language(s): eng - English
 Dates: 2009-11-102009-12-162009-12-222010-05-01
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Structural Biology
  Other : J. Struct. Biol.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Orlando, Fla. : Academic Press
Pages: - Volume / Issue: 170 (2) Sequence Number: - Start / End Page: 307 - 312 Identifier: ISSN: 1047-8477
CoNE: /journals/resource/954922650160