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Haemadin

FieldValue
SymbolHaemadin
NameHaemadin
imagePDB 1e0f EBI.jpg
captioncrystal structure of the human alpha-thrombin-haemadin complex: an exosite ii-binding inhibitor
PfamPF09065
InterProIPR015150
SCOP1e0f

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 antistasin (MEROPS I15).

References

References

  1. (November 2000). "Crystal structure of the human alpha-thrombin-haemadin complex: an exosite II-binding inhibitor". EMBO J..
  2. "InterPro".
  3. "Clan IM".
Wikipedia Source

This article was imported from Wikipedia and is available under the Creative Commons Attribution-ShareAlike 4.0 License. Content has been adapted to SurfDoc format. Original contributors can be found on the article history page.

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