Results 31 to 40 of about 1,281 (179)
Conformational Heterogeneity of Pro-Pro Containing 23-Membered Ring Conopeptides by NMR. [PDF]
Dhurjad P +4 more
europepmc +2 more sources
Conopeptides from the marine cone snails are a mixture of cysteine-rich active peptides, representing a unique and fertile resource for neuroscience research and drug discovery.
Han Zhang +18 more
doaj +1 more source
Current ConoServer database accumulates 8,134 conopeptides from 122 species of cone snail, which are pharmaceutically attractive marine resource. However, many more conopeptides remain to be discovered, and the enzymes involved in their synthesis and ...
Han Zhang +11 more
doaj +1 more source
Cupryphans, metal‐binding, redox‐active, redesigned conopeptides [PDF]
AbstractContryphans are bioactive peptides, isolated from the venom of marine snails of the genus Conus, which are characterized by the short length of the polypeptide chain and the high degree of unusual post‐translational modifications. The cyclization of the polypeptide chain through a single disulphide bond, the presence of two conserved Pro ...
BARBA, MARCO +7 more
openaire +6 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
Hormone-like conopeptides - new tools for pharmaceutical design. [PDF]
Marine cone snails produce an array of hormone-like peptides in their venom, providing bioactive leads for developing peptide drugs and small molecule mimetics.
Turner A, Kaas Q, Craik DJ.
europepmc +5 more sources
Non-Peptidic Small Molecule Components from Cone Snail Venoms
Venomous molluscs (Superfamily Conoidea) comprise a substantial fraction of tropical marine biodiversity (>15,000 species). Prior characterization of cone snail venoms established that bioactive venom components used to capture prey, defend against ...
Zhenjian Lin +14 more
doaj +1 more source
Tyrosine-rich Conopeptides Affect Voltage-gated K+ Channels [PDF]
Two venom peptides, CPY-Pl1 (EU000528) and CPY-Fe1 (EU000529), characterized from the vermivorous marine snails Conus planorbis and Conus ferrugineus, define a new class of conopeptides, the conopeptide Y (CPY) family. The peptides have no disulfide cross-links and are 30 amino acids long; the high content of tyrosine is unprecedented for any native ...
Imperial, Julita S. +7 more
openaire +4 more sources

