ISSN:
1399-0047
Source:
Crystallography Journals Online : IUCR Backfile Archive 1948-2001
Topics:
Chemistry and Pharmacology
,
Geosciences
,
Physics
Notes:
Applaggin (Agkistrodon piscivorus piscivorus platelet-aggregation inhibitor) is a potent inhibitor of blood platelet aggregation derived from the venom of the North American water moccasin. The protein consists of 71 amino acids, is rich in cysteines, contains the sequence-recognition site of adhesion proteins at positions 50–52 (Arg-Gly-Asp) and shares high sequence homology with other snake-venom disintegrins such as echistatin, kistrin and trigramin. Single crystals of applaggin have been grown and X-ray diffraction data have been collected to a resolution of 3.2 Å. The crystals belong to space group P41212 (or its enantiomorph), with unit-cell dimensions a = b = 63.35, c = 74.18 Å and two molecules per asymmetric unit. Molecular replacement using models constructed from the NMR structures of echistatin and kistrin has not been successful in producing a trial structure for applaggin.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1107/S0907444999006332
