Structure Gallery

High resolution membrane protein structures using Salipro® and CryoEM

Salipro® and CryoEM

 

Cryo-electron microscopy (cryoEM) is a cutting-edge technique used in drug discovery and structure-based drug design, as it can deliver key information on drug targets.

The Salipro® technology has been used to solve numerous high resolution structures of membrane proteins with cryoEM.

The images below showcase several of these structures, consisting of the membrane protein (yellow) and Salipro® scaffold protein (blue). In some cases, the membrane protein is bound to ligands (other colors). Click on the images below to learn more.

See our full publication list here.

J. J. Kim, et al., Shared structural mechanisms of general anaesthetics and benzodiazepines. Nature (2020).

J. J. Kim, et al., Shared structural mechanisms of general anaesthetics and benzodiazepines. Nature (2020).

C. M. Noviello, et al., Structural mechanisms of GABAA receptor autoimmune encephalitis. Cell 185, 2469-2477 (2022).

C. M. Noviello, et al., Structural mechanisms of GABAA receptor autoimmune encephalitis. Cell 185, 2469-2477 (2022).

N. X. Nguyen, et al., Cryo-EM structure of a fungal mitochondrial calcium uniporter. Nature 559, 570–574 (2018).

N. X. Nguyen, et al., Cryo-EM structure of a fungal mitochondrial calcium uniporter. Nature 559, 570–574 (2018).

M. M. Rahman, et al., Structure of the Native Muscle-type Nicotinic Receptor and Inhibition by Snake Venom Toxins. Neuron, 1–11 (2020).

M. M. Rahman, et al., Structure of the Native Muscle-type Nicotinic Receptor and Inhibition by Snake Venom Toxins. Neuron, 1–11 (2020).

A. F. Kintzer, et al., Structural basis for activation of voltage sensor domains in an ion channel TPC1. Proc. Natl. Acad. Sci. U. S. A. 115, E9095–E9104 (2018).

A. F. Kintzer, et al., Structural basis for activation of voltage sensor domains in an ion channel TPC1. Proc. Natl. Acad. Sci. U. S. A. 115, E9095–E9104 (2018).

A. Gharpure, et al., Agonist Selectivity and Ion Permeation in the α3β4 Ganglionic Nicotinic Receptor. Neuron 104, 501-511.e6 (2019).

A. Gharpure, et al., Agonist Selectivity and Ion Permeation in the α3β4 Ganglionic Nicotinic Receptor. Neuron 104, 501-511.e6 (2019).

C. M. Noviello, et al., Structure and gating mechanism of the a7 nicotinic acetylcholine receptor. Cell 184, 1–14 (2021).

C. M. Noviello, et al., Structure and gating mechanism of the a7 nicotinic acetylcholine receptor. Cell 184, 1–14 (2021).

Y. Zhang, et al., Asymmetric opening of the homopentameric 5-HT3A serotonin receptor in lipid bilayers. Nat. Commun. 12, 1074 (2021).

Y. Zhang, et al., Asymmetric opening of the homopentameric 5-HT3A serotonin receptor in lipid bilayers. Nat. Commun. 12, 1074 (2021).

D. Du, et al., Interactions of a bacterial RND transporter with a transmembrane small protein in a lipid environment. Struct. Des., 1–10 (2020).

D. Du, et al., Interactions of a bacterial RND transporter with a transmembrane small protein in a lipid environment. Struct. Des., 1–10 (2020).

R. Nagamura, et al., Structural basis for oligomerization of the prokaryotic peptide transporter PepT So2. Acta Crystallogr. Sect. F Struct. Biol. Commun. 75, 348–358 (2019).

R. Nagamura, et al., Structural basis for oligomerization of the prokaryotic peptide transporter PepT So2. Acta Crystallogr. Sect. F Struct. Biol. Commun. 75, 348–358 (2019).

L. Xiao, et al., Structures of the β-barrel assembly machine recognizing outer membrane protein substrates. FASEB J. 35, 1–13 (2021).

L. Xiao, et al., Structures of the β-barrel assembly machine recognizing outer membrane protein substrates. FASEB J. 35, 1–13 (2021).

A. Ornik-cha, et al., Structural and functional analysis of the promiscuous AcrB and AdeB efflux pumps suggests different drug binding mechanisms. Nat. Commun. 12, 6919 (2021).

A. Ornik-cha, et al., Structural and functional analysis of the promiscuous AcrB and AdeB efflux pumps suggests different drug binding mechanisms. Nat. Commun. 12, 6919 (2021).

D.-M. Kehlenbeck, et al., Cryo-EM structure of MsbA in saposin-lipid nanoparticles ( Salipro ) provides insights into nucleotide coordination. FEBS J., 1–12 (2021).

D.-M. Kehlenbeck, et al., Cryo-EM structure of MsbA in saposin-lipid nanoparticles ( Salipro ) provides insights into nucleotide coordination. FEBS J., 1–12 (2021).

M. M. Rahman, et al., Structural mechanism of muscle nicotinic receptor desensitization and block by curare. Nat. Struct. Mol. Biol. 29, 386–394 (2022).

M. M. Rahman, et al., Structural mechanism of muscle nicotinic receptor desensitization and block by curare. Nat. Struct. Mol. Biol. 29, 386–394 (2022).

C. Wang, M. M. Polovitskaya, B. D. Delgado, T. J. Jentsch, S. B. Long, Gating choreography and mechanism of the human proton-activated chloride channel ASOR. Sci. Adv. 8, 1–13 (2022).

C. Wang, M. M. Polovitskaya, B. D. Delgado, T. J. Jentsch, S. B. Long, Gating choreography and mechanism of the human proton-activated chloride channel ASOR. Sci. Adv. 8, 1–13 (2022).

Xu et al., Embigin facilitates monocarboxylate transporter 1 localization to the plasma membrane and transition to a decoupling state. Cell Reports 40, 111343 (2022).

Xu et al., Embigin facilitates monocarboxylate transporter 1 localization to the plasma membrane and transition to a decoupling state. Cell Reports 40, 111343 (2022).