Abstract
Using a combination of genomic and post-genomic approaches is rapidly altering the number of identified human influx carriers. A transmembrane protein bilitranslocase (TCDB 2.A.65) has long attracted attention because of its function as an organic anion carrier. It has also been identified as a potential membrane transporter for cellular uptake of several drugs and due to its implication in drug uptake, it is extremely important to advance the knowledge about its structure. However, at present, only the primary structure of bilitranslocase is known. In our work, transmembrane subunits of bilitranslocase were predicted by a previously developed chemometrics model and the stability of these polypeptide chains were studied by molecular dynamics (MD) simulation. Furthermore, sodium dodecyl sulfate (SDS) micelles were used as a model of cell membrane and herein we present a high-resolution 3D structure of an 18 amino acid residues long peptide corresponding to the third transmembrane part of bilitranslocase obtained by use of multidimensional NMR spectroscopy. It has been experimentally confirmed that one of the transmembrane segments of bilitranslocase has alpha helical structure with hydrophilic amino acid residues oriented towards one side, thus capable of forming a channel in the membrane.
Highlights
Bilitranslocase (BTL) is a plasma membrane protein functioning as an organic anion carrier
The solid state NMR technique is suitable to proteins of higher molecular weight, because in contrast to the solution state, the coherence lifetimes in the solid state are not affected by molecular tumbling [19]
Prediction of BTL Transmembrane Regions The transmembrane region prediction model [23] requires dividing the protein sequence into 20 residues long overlapping segments, each of which is given to the model for prediction
Summary
Bilitranslocase (BTL) is a plasma membrane protein functioning as an organic anion carrier. In the present work the initially predicted transmembrane regions of BTL have been reexamined and we substantiated that 3D structure of one of the transmembrane peptides (TM 3) is alpha helical by MD simulations in the standard DPPC (dipalmitoyl phosphatidyl choline) membrane.
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
