The recognition of membrane-bound PtdIns3P by PX domains

Jia, ZhiGuang, Ghai, Rajesh, Collins, Brett M. and Mark, Alan E. (2014) The recognition of membrane-bound PtdIns3P by PX domains. Proteins: structure, function, and bioinformatics, 82 10: 2332-2342. doi:10.1002/prot.24593

Author Jia, ZhiGuang
Ghai, Rajesh
Collins, Brett M.
Mark, Alan E.
Title The recognition of membrane-bound PtdIns3P by PX domains
Formatted title
The recognition of membrane-bound PtdIns3P by PX domains
Journal name Proteins: structure, function, and bioinformatics   Check publisher's open access policy
ISSN 0887-3585
Publication date 2014-04-26
Year available 2014
Sub-type Article (original research)
DOI 10.1002/prot.24593
Open Access Status Not Open Access
Volume 82
Issue 10
Start page 2332
End page 2342
Total pages 11
Place of publication Hoboken, NJ, United States
Publisher John Wiley & Sons
Language eng
Formatted abstract
Phox-homology (PX) domains target proteins to the organelles of the secretary and endocytic systems by binding to phosphatidylinositol phospholipids (PIPs). Among all the structures of PX domains that have been solved, only three have been solved in a complex with the main physiological ligand: PtdIns3P. In this work, molecular dynamic simulations have been used to explore the structure and dynamics of the p40phox-PX domain and the SNX17-PX domain and their interaction with membrane-bound PtdIns3P. In the simulations, both PX domains associated spontaneously with the membrane-bound PtdIns3P and formed stable complexes. The interaction between the p40phox-PX domain and PtdIns3P in the membrane was found to be similar to the crystal structure of the p40phox-PX-PtdIns3P complex that is available. The interaction between the SNX17-PX domain and PtdIns3P was similar to that observed in the p40phox-PX-PtdIns3P complex, however some residues adopted different orientations. The simulations also showed that non-specific interactions between the β1-β2 loop and the membrane play an important role in the interaction of membrane bound PtdIns3P and different PX domains. The behaviour of unbound PtdIns3P within a 2-oleoyl-1-palmitoyl-sn-glycero-3-phosphocholine (POPC) membrane environment was also examined and compared to the available experimental data and simulation studies of related molecules. 
Keyword Phox-homology proteins
Phosphatidylinositol phospholipids
Molecular simulation
Membrane-binding protein
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes epub ahead of print

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2015 Collection
School of Chemistry and Molecular Biosciences
Institute for Molecular Bioscience - Publications
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 1 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 1 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Wed, 07 May 2014, 19:21:27 EST by Mrs Louise Nimwegen on behalf of School of Chemistry & Molecular Biosciences