Unknown

Dataset Information

0

Advances in NMR structures of integral membrane proteins.


ABSTRACT: Integral membrane proteins (IMPs) play a central role in cell communication with the environment. Their structures are essential for our understanding of the molecular mechanisms of signaling and for drug design, yet they remain badly underrepresented in the protein structure databank. Solution NMR is, aside from X-ray crystallography, the major tool in structural biology. Here we review recently reported solution NMR structures of polytopic IMPs and discuss the new approaches, which were developed in the course of these studies to overcome barriers in the field. Advances in cell-free protein expression, combinatorial isotope labeling, resonance assignment, and collection of structural data greatly accelerated IMP structure determination by solution NMR. In addition, novel membrane-mimicking media made possible determination of solution NMR structures of IMPs in a native-like lipid environment.

SUBMITTER: Maslennikov I 

PROVIDER: S-EPMC3737378 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

Advances in NMR structures of integral membrane proteins.

Maslennikov Innokentiy I   Choe Senyon S  

Current opinion in structural biology 20130527 4


Integral membrane proteins (IMPs) play a central role in cell communication with the environment. Their structures are essential for our understanding of the molecular mechanisms of signaling and for drug design, yet they remain badly underrepresented in the protein structure databank. Solution NMR is, aside from X-ray crystallography, the major tool in structural biology. Here we review recently reported solution NMR structures of polytopic IMPs and discuss the new approaches, which were develo  ...[more]

Similar Datasets

| S-EPMC5314686 | biostudies-literature
| S-EPMC31918 | biostudies-literature
| S-EPMC3664232 | biostudies-literature
| S-EPMC2780624 | biostudies-literature
| S-EPMC10042369 | biostudies-literature
| S-EPMC3770350 | biostudies-literature
| S-EPMC2374085 | biostudies-literature
| S-EPMC4018139 | biostudies-literature
| S-EPMC8627552 | biostudies-literature
| S-EPMC3604715 | biostudies-literature