dbo:abstract
|
- A cystine knot is a protein structural motif containing three disulfide bridges (formed from pairs of cysteine residues). The sections of polypeptide that occur between two of them form a loop through which a third disulfide bond passes, forming a rotaxane substructure. The cystine knot motif stabilizes protein structure and is conserved in proteins across various species. There are three types of cystine knot, which differ in the topology of the disulfide bonds:
* The growth factor cystine knot (GFCK)
* inhibitor cystine knot (ICK) common in spider and snail toxins
* Cyclic Cystine Knot, or cyclotide The growth factor cystine knot was first observed in the structure of nerve growth factor (NGF), solved by X-ray crystallography and published in 1991 by Tom Blundell in Nature. The GFCK is present in four superfamilies. These include nerve growth factor, transforming growth factor beta (TGF-β), platelet-derived growth factor, and glycoprotein hormones including human chorionic gonadotropin. These are structurally related due to the presence of the cystine knot motif but differ in sequence. All GFCK structures that have been determined are dimeric, but their dimerization modes in different classes are different. The vascular endothelial growth factor subfamily, categorized as part of the platelet-derived growth factor superfamily, includes proteins that are angiogenic factors. The presence of the cyclic cystine knot (CCK) motif was discovered when cyclotides were isolated from various plant families. The CCK motif has a cyclic backbone, triple stranded beta sheet, and cystine knot conformation. Novel proteins are being added to the cystine knot motif family, also known as the C-terminal cystine knot (CTCK) proteins. They share approximately 90 amino acid residues in their cysteine-rich C-terminal regions. Inhibitor cystine knot (ICK) is a structural motif with a triple stranded antiparallel beta sheet linked by three disulfide bonds, forming a knotted core. The ICK motif can be found under the category of phylum, such as animals and plants. It is often found in many venom peptides such as those of snails, spiders, and scorpions. Peptide K-PVIIA, which contains an ICK, can undergo a successful enzymatic backbone cyclization. The disulfide connectivity and the common sequence pattern of the ICK motif provides the stability of the peptides that support cyclization. (en)
- Der Cystin-Knoten (engl. cystine knot) ist eine Proteinstruktur, die aus drei Disulfidbrücken gebildet wird (d. h. aus drei Paaren von Cystein-Aminosäureresten).Die Polypeptidkette zwischen zwei dieser Disulfidbrücken bildet einen Ring, durch den die dritte Disulfidbrücke führt (sogenannte Rotaxan-Struktur). Cystin-Knoten kommen in vielen Proteinen vor und stabilisieren die Tertiärstruktur des Proteins. Es werden drei verschiedene Typen von Cystin-Knoten unterschieden, die sich in der Topologie der Disulfidbrücken unterscheiden:
* Wachstumsfaktor-Cystin-Knoten (engl. Growth Factor Cystine Knot, GFCK)
* Inhibitor-Cystin-Knoten (engl. inhibitor cystine knot, ICK), der in Spinnen und Schneckengiften häufig anzutreffen ist
* Zyklischer Cystin-Knoten (engl. cyclic cystine knot oder cyclotide) Der Wachstumsfaktor-Cystin-Knoten (GFCK) wurde erstmals is der Struktur des Nervenwachstumsfaktors beschrieben, die 1991 durch Kristallstrukturanalyse von bestimmt wurde. Alle bisher bekannten GFCK-Strukturen sind dimer, aber sie unterscheiden sich in der Art und Weise der Dimerisierung. (de)
- Un pont cystine est un pont disulfure entre deux résidus de cystéine, un acide aminé protéinogène.[Quoi ?] (fr)
- Un ponte cistina, o nodo di cistina, è una struttura supersecondaria rappresentata dal legame disolfuro (-S-S-) tra due molecole di cisteina facenti parte di uno stesso polipeptide. La sezione di polipeptide in cui è presente il ponte cistina forma un "nodo" attraverso il quale passa un terzo legame disolfuro. È presente in molte strutture proteiche alle quali fornisce una considerevole stabilità strutturale. (it)
|
dbo:symbol
| |
dbo:thumbnail
| |
dbo:wikiPageID
| |
dbo:wikiPageLength
|
- 9045 (xsd:nonNegativeInteger)
|
dbo:wikiPageRevisionID
| |
dbo:wikiPageWikiLink
| |
dbp:caption
|
- Structure of human chorionic gonadotropin. (en)
|
dbp:interpro
| |
dbp:name
| |
dbp:pdb
| |
dbp:pfam
| |
dbp:pfamClan
| |
dbp:scop
| |
dbp:symbol
| |
dbp:wikiPageUsesTemplate
| |
dcterms:subject
| |
gold:hypernym
| |
rdf:type
| |
rdfs:comment
|
- Un pont cystine est un pont disulfure entre deux résidus de cystéine, un acide aminé protéinogène.[Quoi ?] (fr)
- Un ponte cistina, o nodo di cistina, è una struttura supersecondaria rappresentata dal legame disolfuro (-S-S-) tra due molecole di cisteina facenti parte di uno stesso polipeptide. La sezione di polipeptide in cui è presente il ponte cistina forma un "nodo" attraverso il quale passa un terzo legame disolfuro. È presente in molte strutture proteiche alle quali fornisce una considerevole stabilità strutturale. (it)
- Der Cystin-Knoten (engl. cystine knot) ist eine Proteinstruktur, die aus drei Disulfidbrücken gebildet wird (d. h. aus drei Paaren von Cystein-Aminosäureresten).Die Polypeptidkette zwischen zwei dieser Disulfidbrücken bildet einen Ring, durch den die dritte Disulfidbrücke führt (sogenannte Rotaxan-Struktur). Cystin-Knoten kommen in vielen Proteinen vor und stabilisieren die Tertiärstruktur des Proteins. Es werden drei verschiedene Typen von Cystin-Knoten unterschieden, die sich in der Topologie der Disulfidbrücken unterscheiden: (de)
- A cystine knot is a protein structural motif containing three disulfide bridges (formed from pairs of cysteine residues). The sections of polypeptide that occur between two of them form a loop through which a third disulfide bond passes, forming a rotaxane substructure. The cystine knot motif stabilizes protein structure and is conserved in proteins across various species. There are three types of cystine knot, which differ in the topology of the disulfide bonds: (en)
|
rdfs:label
|
- Cystin-Knoten (de)
- Cystine knot (en)
- Pont cystine (fr)
- Ponte cistina (it)
|
owl:sameAs
| |
prov:wasDerivedFrom
| |
foaf:depiction
| |
foaf:isPrimaryTopicOf
| |
is dbo:wikiPageRedirects
of | |
is dbo:wikiPageWikiLink
of | |
is foaf:primaryTopic
of | |