1.45 Å resolution structure of SRPN18 from the malaria vector Anopheles gambiae
作者： David A. Meekins , Xin Zhang , Kevin P. Battaile , Scott Lovell , Kristin Michel
DOI: 10.1107/S2053230X16017854
关键词:
摘要: Serine protease inhibitors (serpins) in insects function within development, wound healing and immunity. The genome of the African malaria vector, Anopheles gambiae, encodes 23 distinct serpin proteins, several which are implicated disease-relevant physiological responses. A. gambiae 18 (SRPN18) was previously categorized as non-inhibitory based on sequence its reactive-center loop (RCL), a region responsible for targeting initiating inhibition. crystal structure SRPN18 determined to resolution 1.45 A, including nearly entire RCL one two molecules asymmetric unit. reveals that is extremely short constricted, feature associated with noncanonical or superfamily members. Furthermore, does not contain suitable target site contains large number prolines. therefore unique architecture among highly conserved fold.
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