Diez, Gerold and List, Felix and Smith, James and Ziegler, Wolfgang H. and Goldmann, Wolfgang H. (2008) Direct evidence of vinculin tail-lipid membrane interaction in beta-sheet conformation. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 373 (1). pp. 69-73. ISSN 0006-291X,
Full text not available from this repository. (Request a copy)Abstract
The focal adhesion protein vinculin (1066 residues) plays an important role in cell adhesion and migration. The interaction between vinculin and lipid membranes is necessary to ensure these processes. There are three putative lipid-membrane interaction sites located at the vinculin tail domain two that form amphipathic alpha-helices (residues 935-978 and 1020-1040) and one that remains unstructured (residues 1052-1066) during crystallization. In this work, the structural and biochemical properties of the last 21 residues of the vinculin tail domain were investigated. Differential scanning calorimetry was performed in the presence of lipid vesicles consisting of dimyristoyl-L-alpha-phosphatidylcholine and dimyristoyl-L-alpha-phosphatidylglycerol at various molar ratios. The results demonstrate that this peptide inserts into lipid vesicle membranes. Examining the secondary structure of this peptide by molecular dynamics simulations and circular dichroism Spectroscopy, we show that it adopts an antiparallel beta sheet backbone geometry that could ensure the association with lipid vesicles. (C) 2008 Elsevier Inc. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PROTEIN SECONDARY STRUCTURE; ACIDIC PHOSPHOLIPIDS; TALIN; ADHESION; BINDING; DOMAIN; ACTIN; ASSOCIATION; ACTIVATION; DICHROWEB; vinculin; vinculin tail carboxy-terminal peptide; lipid membrane binding; focal adhesion complex; molecular dynamics simulation; differential scanning calorimetry; circular dichroism spectroscopy |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 26 Oct 2020 09:34 |
| Last Modified: | 26 Oct 2020 09:34 |
| URI: | https://pred.uni-regensburg.de/id/eprint/30475 |
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