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The recognition of membrane‐bound PtdIns3P by PX domains

Overview of attention for article published in Proteins: Structure, Function, and Bioinformatics, May 2014
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Title
The recognition of membrane‐bound PtdIns3P by PX domains
Published in
Proteins: Structure, Function, and Bioinformatics, May 2014
DOI 10.1002/prot.24593
Pubmed ID
Authors

ZhiGuang Jia, Rajesh Ghai, Brett M. Collins, Alan E. Mark

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 p40(phox) -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 p40(phox) -PX domain and PtdIns3P in the membrane was found to be similar to the crystal structure of the p40(phox) -PX-PtdIns3P complex that is available. The interaction between the SNX17-PX domain and PtdIns3P was similar to that observed in the p40(phox) -PX-PtdIns3P complex; however, some residues adopted different orientations. The simulations also showed that nonspecific 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.

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Mendeley readers

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The data shown below were compiled from readership statistics for 22 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 22 100%

Demographic breakdown

Readers by professional status Count As %
Student > Master 4 18%
Student > Ph. D. Student 4 18%
Researcher 3 14%
Student > Bachelor 3 14%
Other 1 5%
Other 2 9%
Unknown 5 23%
Readers by discipline Count As %
Agricultural and Biological Sciences 11 50%
Biochemistry, Genetics and Molecular Biology 4 18%
Pharmacology, Toxicology and Pharmaceutical Science 1 5%
Medicine and Dentistry 1 5%
Unknown 5 23%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 26 April 2014.
All research outputs
#20,656,820
of 25,374,917 outputs
Outputs from Proteins: Structure, Function, and Bioinformatics
#2,748
of 3,332 outputs
Outputs of similar age
#177,946
of 241,837 outputs
Outputs of similar age from Proteins: Structure, Function, and Bioinformatics
#36
of 63 outputs
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