Journal ArticleDOI
The cystine knot structure of ion channel toxins and related polypeptides
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TLDR
The compact and robust nature of this motif makes it an excellent scaffold for the design and engineering of novel polypeptides with enhanced activity against existing targets, or with activity against novel targets.Citations
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Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif
TL;DR: The structural features of the two apparent subfamilies of the CCK peptides which may be significant for the likely defense related role of these peptides within plants are defined.
Journal ArticleDOI
Isolation of a tarantula toxin specific for a class of proton-gated Na+ channels.
Pierre Escoubas,Pierre Escoubas,Jan de Weille,Alain Lecoq,Sylvie Diochot,Rainer Waldmann,Guy Champigny,Danielle Moinier,André Ménez,Michel Lazdunski +9 more
TL;DR: A novel 40-amino acid toxin from tarantula venom is described, which potently blocks a particular subclass of ASIC channels that are highly expressed in both central nervous system neurons and sensory neurons from dorsal root ganglia.
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The cystine knot motif in toxins and implications for drug design.
TL;DR: The stability of peptide toxins containing the cystine knot motif, their range of bioactivities and their unique structural scaffold can be harnessed for molecular engineering applications and in drug design.
Journal ArticleDOI
The Expanding Social Network of Ionotropic Glutamate Receptors: TARPs and Other Transmembrane Auxiliary Subunits
TL;DR: Pivotal developments in the understanding of the role of TARPs in AMPA receptor trafficking and gating are reviewed, and an overview of how newly discovered transmembrane proteins expand the view of iGluR function in the CNS is provided.
Journal ArticleDOI
Identification of a peptide toxin from Grammostola spatulata spider venom that blocks cation-selective stretch-activated channels.
Thomas M. Suchyna,Janice H. Johnson,Katherine Hamer,Joseph F. Leykam,Douglas A. Gage,Henry F. Clemo,Clive M. Baumgarten,Frederick Sachs +7 more
TL;DR: A 35 amino acid peptide toxin of the inhibitor cysteine knot family that blocks cationic stretch-activated ion channels is identified and implicates SACs in volume regulation.
References
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Journal ArticleDOI
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
TL;DR: The MOLSCRIPT program as discussed by the authors produces plots of protein structures using several different kinds of representations, including simple wire models, ball-and-stick models, CPK models and text labels.
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The Protein Data Bank: a computer-based archival file for macromolecular structures.
Frances C. Bernstein,Thomas F. Koetzle,Graheme J. B. Williams,Edgar F. Meyer,Michael D. Brice,John R. Rodgers,O. Kennard,Takehiko Shimanouchi,Mitsuo Tasumi +8 more
TL;DR: The Protein Data Bank is a computer-based archival file for macromolecular structures that stores in a uniform format atomic co-ordinates and partial bond connectivities, as derived from crystallographic studies.
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A structural superfamily of growth factors containing a cystine knot motif.
TL;DR: The determination of the crystal structure of dimeric NGF revealed a novel three-dimensional fold that contains a cystine knot motif and the evolutionary and functional implications that arise are discussed here.
Journal ArticleDOI
A common structural motif incorporating a cystine knot and a triple-stranded beta-sheet in toxic and inhibitory polypeptides.
TL;DR: This structural motif appears to be one of the smallest stable globular domains found in proteins and is commonly used in toxins and inhibitors that act by blocking the function of larger protein receptors such as ion channels or proteases.
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Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing.
TL;DR: The solution structure of a synthetic 36-residue polypeptide comprising the C-terminal cellulose binding domain of cellobiohydrolase I (CT-CBH I) from Trichoderma reesei was investigated by nuclear magnetic resonance (NMR) spectroscopy.