ArticleJournal of computer-aided molecular design2008
Modeling dimerizations of transmembrane proteins using Brownian dynamics simulations.
Article in Journal of computer-aided molecular design, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- Mechanisms in Thyroid Eye Disease: The TSH Receptor Interacts Directly With the IGF-1 Receptor.Endocrinology · 2025Article
- Modeling TSH Receptor Dimerization at the Transmembrane Domain.Endocrinology · 2022Article
- Methods used to study the oligomeric structure of G-protein-coupled receptors.Bioscience reports · 2017Review
- Allosteric signaling through an mGlu2 and 5-HT2A heteromeric receptor complex and its potential contribution to schizophrenia.Science signaling · 2016Article
- Transmembrane domains of attraction on the TSH receptor.Endocrinology · 2015Article
- Computational approaches for modeling GPCR dimerization.Current pharmaceutical biotechnology · 2014Review
- The free energy landscape of dimerization of a membrane protein, NanC.PLoS computational biology · 2014Article
- Predicting protein interactions by Brownian dynamics simulations.Journal of biomedicine & biotechnology · 2012Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The dimerizations of membrane proteins, Outer Membrane Phospholipase A (OMPLA) and glycophorin A (GPA), have been simulated by an adapted Brownian Dynamics program. To mimic the membrane protein environment, we introduced a hybrid electrostatic potential map of membrane and water for electrostatic interaction calculations. We added a van der Waals potential term to the force field of the current version of the BD program to simulate the short-range interactions of the two monomers. We reduced the BD sampling space from three dimensions to two dimensions to improve the efficiency of BD simulations for membrane proteins. The OMPLA and GPA dimers predicted by our 2D-BD simulation and structural refinement is in good agreement with the experimental structures. The adapted 2D-BD method could be used for prediction of dimerization of other membrane proteins, such as G protein-coupled receptors, to help better understanding of the structures and functions of membrane proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.