The three-dimensional structure of an H-superfamily conotoxin reveals a granulin fold arising from a common ICK cysteine framework

Venomous marine cone snails produce peptide toxins (conotoxins) that bind ion channels and receptors with high specificity and therefore are important pharmacological tools. Conotoxins contain conserved cysteine residues that form disulfide bonds that stabilize their structures. To gain structural i...

Täydet tiedot

Tallennettuna:
Bibliografiset tiedot
Julkaisussa:J Biol Chem
Päätekijät: Nielsen, Lau D., Foged, Mads M., Albert, Anastasia, Bertelsen, Andreas B., Søltoft, Cecilie L., Robinson, Samuel D., Petersen, Steen V., Purcell, Anthony W., Olivera, Baldomero M., Norton, Raymond S., Vasskog, Terje, Safavi-Hemami, Helena, Teilum, Kaare, Ellgaard, Lars
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: American Society for Biochemistry and Molecular Biology 2019
Aiheet:
Protein Structure and Folding
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC6552430/
https://ncbi.nlm.nih.gov/pubmed/30975904
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.RA119.007491
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