tailieunhanh - Báo cáo y học: "CapZ-lipid membrane interactions: a computer analysis"

Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học quốc tế cung cấp cho các bạn kiến thức về ngành y đề tài:CapZ-lipid membrane interactions: a computer analysis | Theoretical Biology and Medical Modelling BioMed Central Research CapZ-lipid membrane interactions a computer analysis James Smith Gerold Diez Anna H Klemm Vitali Schewkunow and Wolfgang H Goldmann Open Access Address Friedrich-Alexander-University of Erlangen-Nuremberg Center for Medical Physics and Technology Biophysics Group Henkestrasse 91 91052 Erlangen Germany Email James Smith - jsmith@ Gerold Diez - gdiez@ Anna H Klemm - aklemm@ Vitali Schewkunow - vschewkunow@ Wolfgang H Goldmann - wgoldmann@ Corresponding author Published 16 August 2006 Received 09 April 2006 Theoretical Biology and Medical Modelling 2006 3 30 doi 1742-4682-3-30 Accepted 16 August 2006 This article is available from http content 3 1 30 2006 Smith et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Background CapZ is a calcium-insensitive and lipid-dependent actin filament capping protein the main function of which is to regulate the assembly of the actin cytoskeleton. CapZ is associated with membranes in cells and it is generally assumed that this interaction is mediated by polyphosphoinositides PPI particularly PIP2 which has been characterized in vitro. Results We propose that non-PPI lipids also bind CapZ. Data from computer-aided sequence and structure analyses further suggest that CapZ could become partially buried in the lipid bilayer probably under mildly acidic conditions in a manner that is not only dependent on the presence of PPIs. We show that lipid binding could involve a number of sites that are spread throughout the CapZ molecule . alpha- and beta-subunits. However a beta-subunit segment