Cardiolipin Interactions with Proteins

Joan Planas-Iglesias, Himal Dwarakanath, Dariush Mohammadyani, Naveena Yanamala, Valerian E. Kagan, Judith Klein-Seetharaman

Research output: Contribution to journalArticlepeer-review

76 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1282-1294
Number of pages13
JournalBiophysical journal
Volume109
Issue number6
DOIs
StatePublished - Sep 19 2015
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics

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