Dataset Information

TMPL: a database of experimental and theoretical transmembrane protein models positioned in the lipid bilayer.

ABSTRACT: Knowing the position of protein structures within the membrane is crucial for fundamental and applied research in the field of molecular biology. Only few web resources propose coordinate files of oriented transmembrane proteins, and these exclude predicted structures, although they represent the largest part of the available models. In this article, we present TMPL (http://www.dsimb.inserm.fr/TMPL/), a database of transmembrane protein structures (?-helical and ?-sheet) positioned in the lipid bilayer. It is the first database to include theoretical models of transmembrane protein structures, making it a large repository with more than 11 000 entries. The TMPL database also contains experimentally solved protein structures, which are available as either atomistic or coarse-grained models. A unique feature of TMPL is the possibility for users to update the database by uploading, through an intuitive web interface, the membrane assignments they can obtain with our recent OREMPRO web server.

SUBMITTER: Postic G

PROVIDER: S-EPMC5467549 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature

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TMPL: a database of experimental and theoretical transmembrane protein models positioned in the lipid bilayer.

Postic Guillaume G Ghouzam Yassine Y Etchebest Catherine C Gelly Jean-Christophe JC

Database : the journal of biological databases and curation 20170101 1

Knowing the position of protein structures within the membrane is crucial for fundamental and applied research in the field of molecular biology. Only few web resources propose coordinate files of oriented transmembrane proteins, and these exclude predicted structures, although they represent the largest part of the available models. In this article, we present TMPL (http://www.dsimb.inserm.fr/TMPL/), a database of transmembrane protein structures (α-helical and β-sheet) positioned in the lipid ...[more]

PMID: 28365741

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Project description:The ligand-binding sites of many G protein-coupled receptors (GPCRs) are situated around and deeply embedded within the central pocket formed by their seven transmembrane-spanning ?-helical domains. Generally, these binding sites are assumed accessible to endogenous ligands from the aqueous phase. Recent advances in the structural biology of GPCRs, along with biophysical and computational studies, suggest that amphiphilic and lipophilic molecules may gain access to these receptors by first partitioning into the membrane and then reaching the binding site via lateral diffusion through the lipid bilayer. In addition, several crystal structures of class A and class B GPCRs bound to their ligands offer unprecedented details on the existence of lipid-facing allosteric binding sites outside the transmembrane helices that can only be reached via lipid pathways. The highly organized structure of the lipid bilayer may direct lipophilic or amphiphilic drugs to a specific depth within the bilayer, changing local concentration of the drug near the binding site and affecting its binding kinetics. Additionally, the constraints of the lipid bilayer, including its composition and biophysical properties, may play a critical role in "pre-organizing" ligand molecules in an optimal orientation and conformation to facilitate receptor binding. Despite its clear involvement in molecular recognition processes, the critical role of the membrane in binding ligands to lipid-exposed transmembrane binding sites remains poorly understood and warrants comprehensive investigation. Understanding the mechanistic basis of the structure-membrane interaction relationship of drugs will not only provide useful insights about receptor binding kinetics but will also enhance our ability to take advantage of the apparent membrane contributions when designing drugs that target transmembrane proteins with improved efficacy and safety. In this minireview, we summarize recent structural and computational studies on membrane contributions to binding processes, elucidating both lipid pathways of ligand access and binding mechanisms for several orthosteric and allosteric ligands of class A and class B GPCRs.

Dataset Information

TMPL: a database of experimental and theoretical transmembrane protein models positioned in the lipid bilayer.

Publications

TMPL: a database of experimental and theoretical transmembrane protein models positioned in the lipid bilayer.

Similar Datasets

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