Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Help & Advice
University of Warwick

The Library

  • Login
  • Admin

Cardiolipin interactions with proteins

Tools
- Tools
+ Tools

Planas-Iglesias, Joan, Dwarakanath, Himal, Mohammadyani, Dariush, Yanamala, Naveena, Kagan, Valerian E and Klein-Seetharaman, Judith (2015) Cardiolipin interactions with proteins. Biophysical Journal, 109 (6). pp. 1282-94. doi:10.1016/j.bpj.2015.07.034

Research output not available from this repository, contact author.
Official URL: http://dx.doi.org/10.1016/j.bpj.2015.07.034

Request Changes to record.

Abstract

Cardiolipins (CL) represent unique phospholipids of bacteria and eukaryotic mitochondria with four acyl chains and two phosphate groups that have been implicated in numerous functions from energy metabolism to apoptosis. Many proteins are known to interact with CL, and several cocrystal structures of protein-CL complexes exist. In this work, we describe the collection of the first systematic and, to the best of our knowledge, the comprehensive gold standard data set of all known CL-binding proteins. There are 62 proteins in this data set, 21 of which have nonredundant crystal structures with bound CL molecules available. Using binding patch analysis of amino acid frequencies, secondary structures and loop supersecondary structures considering phosphate and acyl chain binding regions together and separately, we gained a detailed understanding of the general structural and dynamic features involved in CL binding to proteins. Exhaustive docking of CL to all known structures of proteins experimentally shown to interact with CL demonstrated the validity of the docking approach, and provides a rich source of information for experimentalists who may wish to validate predictions.

Item Type: Journal Article
Divisions: Faculty of Medicine > Warwick Medical School > Biomedical Sciences > Translational & Experimental Medicine > Metabolic and Vascular Health (- until July 2016)
Faculty of Medicine > Warwick Medical School
Journal or Publication Title: Biophysical Journal
Publisher: Biophysical Society
ISSN: 0006-3495
Official Date: 15 September 2015
Dates:
DateEvent
15 September 2015Published
20 August 2015Available
13 July 2015Accepted
19 March 2015Submitted
Volume: 109
Number: 6
Page Range: pp. 1282-94
DOI: 10.1016/j.bpj.2015.07.034
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access
Funder: International Human Frontier Science Program Organization, National Institutes of Health (U.S.) (NIH)
Grant number: HFSP-RGP0013/2014

Request changes or add full text files to a record

Repository staff actions (login required)

View Item View Item
twitter

Email us: wrap@warwick.ac.uk
Contact Details
About Us