Transmembrane recognition of the semaphorin co-receptors neuropilin 1 and plexin A1: coarse-grained simulations

The cancer associated class 3 semaphorins require direct binding to neuropilins and association to plexins to trigger cell signaling. Here, we address the role of the transmembrane domains of neuropilin 1 and plexin A1 for the dimerization of the two receptors by characterizing the assembly in lipid...

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Bibliographic Details
Published in:	PloS one Vol. 9; no. 5; p. e97779
Main Authors:	Aci-Sèche, Samia, Sawma, Paul, Hubert, Pierre, Sturgis, James N, Bagnard, Dominique, Jacob, Laurent, Genest, Monique, Garnier, Norbert
Format:	Journal Article
Language:	English
Published:	United States Public Library of Science 23-05-2014 Public Library of Science (PLoS)
Subjects:	Assembly Biology and Life Sciences Cancer Cell Membrane - metabolism Chemical compounds Dimerization Drug development Handedness Helices Humans Hybrid systems Kinases Life Sciences Ligands Lipid bilayers Lipid Bilayers - chemistry Lipid Bilayers - metabolism Molecular dynamics Molecular Dynamics Simulation Monomers Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - metabolism Neuropilin Neuropilin-1 - chemistry Neuropilin-1 - metabolism Packing Pharmacology Phosphatidylcholines - metabolism Protein Multimerization Protein Structure, Quaternary Proteins Receptors Receptors, Cell Surface - chemistry Receptors, Cell Surface - metabolism Self-association Semaphorins Semaphorins - metabolism Signal transduction Signaling Simulation Thermodynamics Transmembrane domains France Transmembrane receptors Lipids Sequence motif analysis Dimerization Biochemical simulations Free energy Dimers (Chemical physics) Membrane receptor signaling
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