| http://dbpedia.org/ontology/abstract
|
Tachystatins are antimicrobial chitin-bind … Tachystatins are antimicrobial chitin-binding peptides from Japanese horseshoe crab. Amino acid residues Tyr(14) and Arg(17) in Tachystatin B are thought to be the essential residues for chitin binding. These small proteins contain a cysteine-stabilised triple-stranded beta-sheet with an inhibitor cystine knot motif and show features common to membrane-interactive peptides. Tachystatin A is thought to have an antimicrobial activity similar to defensins.timicrobial activity similar to defensins.
|
| http://dbpedia.org/ontology/symbol
|
Tachystatin_A
, Tachystatin_B
|
| http://dbpedia.org/ontology/thumbnail
|
http://commons.wikimedia.org/wiki/Special:FilePath/PDB_1cix_EBI.jpg?width=300 +
|
| http://dbpedia.org/ontology/wikiPageID
|
36358581
|
| http://dbpedia.org/ontology/wikiPageLength
|
2140
|
| http://dbpedia.org/ontology/wikiPageRevisionID
|
996000715
|
| http://dbpedia.org/ontology/wikiPageWikiLink
|
http://dbpedia.org/resource/Beta-sheet +
, http://dbpedia.org/resource/Category:Protein_families +
, http://dbpedia.org/resource/Inhibitor_cystine_knot +
, http://dbpedia.org/resource/Defensins +
, http://dbpedia.org/resource/Peptide +
, http://dbpedia.org/resource/Chitin +
, http://dbpedia.org/resource/Tachypleus_tridentatus +
, http://dbpedia.org/resource/Residue_%28chemistry%29 +
|
| http://dbpedia.org/property/caption
|
Three-dimensional structure of antimicrobial peptide tachystatin A. PDB entry
|
| http://dbpedia.org/property/interpro
|
IPR020957
, IPR022717
|
| http://dbpedia.org/property/name
|
Tachystatin_B
, Tachystatin_A
|
| http://dbpedia.org/property/opmFamily
|
112
|
| http://dbpedia.org/property/opmProtein
|
2
|
| http://dbpedia.org/property/pfam
|
PF11478
, PF11406
|
| http://dbpedia.org/property/pfamClan
|
CL0083
|
| http://dbpedia.org/property/symbol
|
Tachystatin_A
, Tachystatin_B
|
| http://dbpedia.org/property/wikiPageUsesTemplate
|
http://dbpedia.org/resource/Template:InterPro_content +
, http://dbpedia.org/resource/Template:Reflist +
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|
| http://purl.org/dc/terms/subject
|
http://dbpedia.org/resource/Category:Protein_families +
|
| http://purl.org/linguistics/gold/hypernym
|
http://dbpedia.org/resource/Peptides +
|
| http://www.w3.org/ns/prov#wasDerivedFrom
|
http://en.wikipedia.org/wiki/Tachystatin?oldid=996000715&ns=0 +
|
| http://xmlns.com/foaf/0.1/depiction
|
http://commons.wikimedia.org/wiki/Special:FilePath/PDB_1cix_EBI.jpg +
|
| http://xmlns.com/foaf/0.1/isPrimaryTopicOf
|
http://en.wikipedia.org/wiki/Tachystatin +
|
| owl:sameAs |
http://rdf.freebase.com/ns/m.0k3ndnr +
, http://dbpedia.org/resource/Tachystatin +
, http://www.wikidata.org/entity/Q7673880 +
, http://yago-knowledge.org/resource/Tachystatin +
, https://global.dbpedia.org/id/4va9x +
|
| rdf:type |
http://dbpedia.org/class/yago/SocialGroup107950920 +
, http://dbpedia.org/class/yago/Organization108008335 +
, http://dbpedia.org/ontology/Protein +
, http://www.wikidata.org/entity/Q206229 +
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|
| rdfs:comment |
Tachystatins are antimicrobial chitin-bind … Tachystatins are antimicrobial chitin-binding peptides from Japanese horseshoe crab. Amino acid residues Tyr(14) and Arg(17) in Tachystatin B are thought to be the essential residues for chitin binding. These small proteins contain a cysteine-stabilised triple-stranded beta-sheet with an inhibitor cystine knot motif and show features common to membrane-interactive peptides. Tachystatin A is thought to have an antimicrobial activity similar to defensins.timicrobial activity similar to defensins.
|
| rdfs:label |
Tachystatin
|
