| http://dbpedia.org/ontology/abstract
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In molecular biology, haemadin is an antic … In molecular biology, haemadin is an anticoagulant peptide synthesised by the Indian leech, Haemadipsa sylvestris.It adopts a secondary structure consisting of five short beta-strands (beta1-beta5), which are arranged in two antiparallel distorted sheets formed by strands beta1-beta4-beta5 and beta2-beta3 facing each other. This beta-sandwich is stabilised by six enclosed cysteines arranged in a [1-2, 3-5, 4-6] disulfide pairing resulting in a disulfide-rich hydrophobic core that is largely inaccessible to bulk solvent. The close proximity of disulfide bonds [3-5] and [4-6] organises haemadin into four distinct loops. The N-terminal segment of this domain binds to the active site of thrombin, inhibiting it. Haemadin (MEROPS I14.002) belongs to a superfamily (MEROPS IM) of protease inhibitors that also includes hirudin (MEROPS I14.001) and (MEROPS I15).hirudin (MEROPS I14.001) and (MEROPS I15).
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| http://dbpedia.org/ontology/symbol
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Haemadin
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33395921
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2247
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1087875455
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| http://dbpedia.org/property/caption
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crystal structure of the human alpha-thrombin-haemadin complex: an exosite ii-binding inhibitor
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| http://dbpedia.org/property/interpro
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IPR015150
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| http://dbpedia.org/property/name
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Haemadin
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| http://dbpedia.org/property/pfam
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PF09065
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| http://dbpedia.org/property/scop
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1
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| http://dbpedia.org/property/symbol
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Haemadin
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| rdfs:comment |
In molecular biology, haemadin is an antic … In molecular biology, haemadin is an anticoagulant peptide synthesised by the Indian leech, Haemadipsa sylvestris.It adopts a secondary structure consisting of five short beta-strands (beta1-beta5), which are arranged in two antiparallel distorted sheets formed by strands beta1-beta4-beta5 and beta2-beta3 facing each other. This beta-sandwich is stabilised by six enclosed cysteines arranged in a [1-2, 3-5, 4-6] disulfide pairing resulting in a disulfide-rich hydrophobic core that is largely inaccessible to bulk solvent. The close proximity of disulfide bonds [3-5] and [4-6] organises haemadin into four distinct loops. The N-terminal segment of this domain binds to the active site of thrombin, inhibiting it.he active site of thrombin, inhibiting it.
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| rdfs:label |
Haemadin
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