Conformational Heterogeneity of Pro–Pro Containing 23-Membered Ring Conopeptides by NMR [PDF]
Pooja Dhurjad +4 more
doaj +2 more sources
δ-Conotoxin Structure Prediction and Analysis through Large-Scale Comparative and Deep Learning Modeling Approaches. [PDF]
δ‐Conotoxins are a diverse class of peptides that inhibit the inactivation of voltage‐gated sodium channels – proteins implicated in many human diseases – but which remain poorly characterized. Computational modeling of 18 different δ‐conotoxins using traditional and deep learning techniques uncovers structural features underlying the varying ...
McCarthy S, Gonen S.
europepmc +2 more sources
A Chemoenzymatic Approach To Produce a Cyclic Analogue of the Analgesic Drug MVIIA (Ziconotide)
A chemoenzymatic method has been developed to prepare backbone cyclic analogues of the ω‐conotoxin MVIIA. The most potent cyclic analogue, cM‐7, shows highly improved stability and maintains the activity of the native peptide. Abstract Ziconotide (ω‐conotoxin MVIIA) is an approved analgesic for the treatment of chronic pain.
Yan Zhou +8 more
wiley +2 more sources
ConoDictor: a tool for prediction of conopeptide superfamilies [PDF]
ConoDictor is a tool that enables fast and accurate classification of conopeptides into superfamilies based on their amino acid sequence. ConoDictor combines predictions from two complementary approaches-profile hidden Markov models and generalized profiles. Results appear in a browser as tables that can be downloaded in various formats.
Dominique Koua +7 more
openaire +3 more sources
Side‐chain dynamics of the α1B‐adrenergic receptor determined by NMR via methyl relaxation
Abstract G protein‐coupled receptors (GPCRs) are medically important membrane proteins that sample inactive, intermediate, and active conformational states characterized by relatively slow interconversions (~μs–ms). On a faster timescale (~ps–ns), the conformational landscape of GPCRs is governed by the rapid dynamics of amino acid side chains.
Christian Baumann +8 more
wiley +1 more source
Isolation and structural identification of a new T1-conotoxin with unique disulfide connectivities derived from Conus bandanus [PDF]
Background: Conopeptides are neuropharmacological peptides derived from the venomous salivary glands of cone snails. Among 29 superfamilies based on conserved signal sequences, T-superfamily conotoxins, which belong to the smallest group, include four ...
Nguyen Bao +3 more
doaj +1 more source
High‐resolution crystal structure of the Mu8.1 conotoxin from Conus mucronatus
The crystal structure of the Mu8.1 conotoxin was determined in the high‐symmetry space group I4122 at 1.67 Å resolution. This crystal structure reveals a surface‐exposed Zn2+‐binding site and establishes a hydrogen‐bonding network around Lys55 buried at the dimer interface.Marine cone snails produce a wealth of peptide toxins (conotoxins) that bind ...
Emilie Müller +3 more
wiley +1 more source
ConoServer, a database for conopeptide sequences and structures [PDF]
Abstract Summary: ConoServer is a new database dedicated to conopeptides, a large family of peptides found in the venom of marine snails of the genus Conus. These peptides have an exceptional diversity of sequences and chemical modifications and their ability to block ion channels makes them important as drug leads and tools for ...
Quentin Kaas +4 more
openaire +5 more sources
Mechanisms for Evolving Hypervariability: The Case of Conopeptides [PDF]
Hypervariability is a prominent feature of large gene families that mediate interactions between organisms, such as venom-derived toxins or immunoglobulins. In order to study mechanisms for evolution of hypervariability, we examined an EST-generated assemblage of 170 distinct conopeptide sequences from the venoms of five species of marine Conus snails.
S G, Conticello +5 more
openaire +2 more sources
The Conopeptide αD-FrXXA, an Inhibitor of Voltage-Gated Potassium Channels. [PDF]
The conopeptide αD-FrXXA was previously isolated by our team from the venom of the vermivorous snail Conus fergusoni. This toxin is composed of two chains of 47 amino acids and inhibits neuronal and muscular subtypes of nAChR. In this study, we explored its effects on voltage-gated potassium channels heterologously expressed in Xenopus laevis oocytes ...
Martínez-Hernández L +3 more
europepmc +4 more sources

