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21 January 2022
  » arxiv » q-bio.BM/0411023

 Article overview

Model for processive movement of dynein
Ping Xie ; Shuo-Xing Dou ; Peng-Ye Wang ;
Date 11 Nov 2004
Subject Biomolecules | q-bio.BM
AbstractA model for the processive movement of dynein is presented based on experimental observations available. In the model, the change from strong microtubule-binding to weak binding of dynein is determined naturally by the variation of the relative orientation between the two interacting surfaces of the stalk tip and the microtubule as the stalk rotates from the ADP.Vi-state orientation to the apo-state orientation. This means that the puzzling communication from the ATP binding site in the globular head to the MT-binding site in the tip of the stalk, which is prerequisite in the conventional model, is not required. Using the present model, the previous experimental results, such as (i) the step size of a dynein being an integer times of the period of the MT lattice, (ii) the dependence of the step size on load, i.e., the step size decreasing with the increase of load, and (iii) the stall force being proportional to [ATP] at low [ATP] and becoming saturated at high [ATP], are well explained.
Source arXiv, q-bio.BM/0411023
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