About: Inhibitor cystine knot

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An inhibitor cystine knot (aka ICK or Knottin) is a protein structural motif containing three disulfide bridges. Knottins are one of three folds in the cystine knot motif; the other closely related knots are the Growth Factor Cystine Knot (GFCK) and the Cyclic Cystine Knot (CCK; cyclotide). Types include a) cyclic mobius, b) cyclic bracelet, c) acyclic inhibitor knottins. Cystine knot motifs are found frequently in nature in a plethora of plants, animals, and fungi and serve diverse functions from appetite suppression to anti-fungal activity.

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rdf:type	yago:WikicatNeurotoxins yago:Matter100020827 yago:Neurotoxin115036321 yago:PhysicalEntity100001930 yago:Poison115032376 yago:WikicatIonChannelToxins protein yago:Substance100020090 yago:Toxin115034074
rdfs:label	Inhibitor cystine knot (en)
rdfs:comment	An inhibitor cystine knot (aka ICK or Knottin) is a protein structural motif containing three disulfide bridges. Knottins are one of three folds in the cystine knot motif; the other closely related knots are the Growth Factor Cystine Knot (GFCK) and the Cyclic Cystine Knot (CCK; cyclotide). Types include a) cyclic mobius, b) cyclic bracelet, c) acyclic inhibitor knottins. Cystine knot motifs are found frequently in nature in a plethora of plants, animals, and fungi and serve diverse functions from appetite suppression to anti-fungal activity. (en)
foaf:depiction
dcterms:subject	Cysteine-rich proteins Protein structure Protein folds Neurotoxins Ion channel toxins
Wikipage page ID	41336858 (xsd:integer)
Wikipage revision ID	1121649006 (xsd:integer)
Link from a Wikipage to another Wikipage	Cysteine-rich proteins Cyclotide Vanillotoxin Vejocalcin Double-knot toxin Proteolysis Convergent evolution Arachnid Stromatoxin Denaturation (biochemistry) Hainantoxin Maurocalcine Albumin I Protein structure Cystine knot Protein folds Grammotoxin Hanatoxin Delta-palutoxin Protein Neurotoxins GsMTx-4 Covalitoxin-II Huwentoxin Ion channel toxins Agouti signalling peptide Tachystatin Heteroscodratoxin-1 Guangxitoxin Knot (mathematics) Disulfide bridge TLTx Phrixotoxin Psalmotoxin Agouti related peptide Robustoxin Molluscs
Link from a Wikipage to an external page	https://www.dsimb.inserm.fr/KNOTTIN/ https://web.archive.org/web/20150205045006/http:/cyclotide.com/knots.html
sameAs	Inhibitor cystine knot Inhibitor cystine knot Inhibitor cystine knot Inhibitor cystine knot
dbp:wikiPageUsesTemplate	dbt:Reflist dbt:PDBe
thumbnail	wiki-commons:Special:FilePath/Knottin_Structure.png?width=300
has abstract	An inhibitor cystine knot (aka ICK or Knottin) is a protein structural motif containing three disulfide bridges. Knottins are one of three folds in the cystine knot motif; the other closely related knots are the Growth Factor Cystine Knot (GFCK) and the Cyclic Cystine Knot (CCK; cyclotide). Types include a) cyclic mobius, b) cyclic bracelet, c) acyclic inhibitor knottins. Cystine knot motifs are found frequently in nature in a plethora of plants, animals, and fungi and serve diverse functions from appetite suppression to anti-fungal activity. Along with the sections of polypeptide between them, two disulfides form a loop through which the third disulfide bond (linking the 3rd and 6th cysteine in the sequence) passes, forming a knot. The motif is common in invertebrate toxins such as those from arachnids and molluscs. The motif is also found in some inhibitor proteins found in plants, but the plant and animal motifs are thought to be a product of convergent evolution. The ICK motif is a very stable protein structure which is resistant to heat denaturation and proteolysis.CK peptide components of venoms target voltage-gated ion channels but members of the family also act as antibacterial and haemolytic agents. Plant ICK proteins are often protease inhibitors. Knottins have high stability to pH, heat, and enzymes. Because of their stability and their favorable pharmacodynamic properties, knottins are becoming increasingly popular as protein engineering scaffolds. Moreover, engineered knottins have shown significant promise as therapeutics, imaging agents, and targeting agents for chemotherapy. The mammalian proteins Agouti signalling peptide and Agouti related peptide are the only known mammalian examples of this motif. Both are neuropeptides involved in cell signalling. The former is responsible for hair (fur) colouration. The motif is similar to the cyclic cystine knot or cyclotide, but lacks the cyclisation of the polypeptide backbone which is present in the latter family. The growth factor cystine knot (GFCK) shares the motif but its topology is such that it is the bond between the first and fourth disulfide which threads through the loop. (en)
gold:hypernym	Motif
prov:wasDerivedFrom	wikipedia-en:Inhibitor_cystine_knot?oldid=1121649006&ns=0
page length (characters) of wiki page	6583 (xsd:nonNegativeInteger)
foaf:isPrimaryTopicOf	wikipedia-en:Inhibitor_cystine_knot
is rdfs:seeAlso of	Drosomycin
is Link from a Wikipage to another Wikipage of	Cyclotide Vanillotoxin Vejocalcin Double-knot toxin Intrepicalcin Protoxin-I Protoxin-II Psalmopoeus cambridgei Ptu1 Conotoxin Spider toxin Stromatoxin Delta-Palutoxin Delta atracotoxin Dendrocnide moroides Hadrucalcin Hainantoxin Maurocalcine Agouti-related peptide Agouti-signaling protein GTx1-15 Agelenin Albumin I Cystine knot Grammotoxin GsMTx-4

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