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Title: 1.45 Å resolution structure of SRPN18 from the malaria vector Anopheles gambiae

Abstract

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 of which are implicated in disease-relevant physiological responses.A. gambiaeserpin 18 (SRPN18) was previously categorized as non-inhibitory based on the sequence of its reactive-center loop (RCL), a region responsible for targeting and initiating protease inhibition. The crystal structure ofA. gambiaeSRPN18 was determined to a resolution of 1.45 Å, including nearly the entire RCL in one of the two molecules in the asymmetric unit. The structure reveals that the SRPN18 RCL is extremely short and constricted, a feature associated with noncanonical inhibitors or non-inhibitory serpin superfamily members. Furthermore, the SRPN18 RCL does not contain a suitable protease target site and contains a large number of prolines. The SRPN18 structure therefore reveals a unique RCL architecture among the highly conserved serpin fold.

Authors:
; ; ; ;
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
USDOE; National Institutes of Health (NIH)
OSTI Identifier:
1339722
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F, Structural Biology Communications; Journal Volume: 72; Journal Issue: 12
Country of Publication:
United States
Language:
ENGLISH
Subject:
36 MATERIALS SCIENCE

Citation Formats

Meekins, David A., Zhang, Xin, Battaile, Kevin P., Lovell, Scott, and Michel, Kristin. 1.45 Å resolution structure of SRPN18 from the malaria vector Anopheles gambiae. United States: N. p., 2016. Web. doi:10.1107/S2053230X16017854.
Meekins, David A., Zhang, Xin, Battaile, Kevin P., Lovell, Scott, & Michel, Kristin. 1.45 Å resolution structure of SRPN18 from the malaria vector Anopheles gambiae. United States. doi:10.1107/S2053230X16017854.
Meekins, David A., Zhang, Xin, Battaile, Kevin P., Lovell, Scott, and Michel, Kristin. Sat . "1.45 Å resolution structure of SRPN18 from the malaria vector Anopheles gambiae". United States. doi:10.1107/S2053230X16017854.
@article{osti_1339722,
title = {1.45 Å resolution structure of SRPN18 from the malaria vector Anopheles gambiae},
author = {Meekins, David A. and Zhang, Xin and Battaile, Kevin P. and Lovell, Scott and Michel, Kristin},
abstractNote = {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 of which are implicated in disease-relevant physiological responses.A. gambiaeserpin 18 (SRPN18) was previously categorized as non-inhibitory based on the sequence of its reactive-center loop (RCL), a region responsible for targeting and initiating protease inhibition. The crystal structure ofA. gambiaeSRPN18 was determined to a resolution of 1.45 Å, including nearly the entire RCL in one of the two molecules in the asymmetric unit. The structure reveals that the SRPN18 RCL is extremely short and constricted, a feature associated with noncanonical inhibitors or non-inhibitory serpin superfamily members. Furthermore, the SRPN18 RCL does not contain a suitable protease target site and contains a large number of prolines. The SRPN18 structure therefore reveals a unique RCL architecture among the highly conserved serpin fold.},
doi = {10.1107/S2053230X16017854},
journal = {Acta Crystallographica. Section F, Structural Biology Communications},
number = 12,
volume = 72,
place = {United States},
year = {Sat Nov 19 00:00:00 EST 2016},
month = {Sat Nov 19 00:00:00 EST 2016}
}