1.45 Å resolution structure of SRPN18 from the malaria vector<i>Anopheles gambiae</i>

Meekins, David A.; Zhang, Xin; Battaile, Kevin P.; Lovell, Scott; Michel, Kristin

doi:10.1107/s2053230x16017854

Cited by 3 publications

(3 citation statements)

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“…The RCL in serpins is a solvent-exposed region between strand-4A and strand-1C, consisting of 16–25 amino acid residues (Meekins et al ., 2016). In the inhibition of a proteinase by a serpin, the proteinase cleaves the RCL at a specific position called the scissile bond, between two residues designated P1 and P1’ (Loebermann et al ., 1984).…”

Section: Resultsmentioning

confidence: 99%

The Manduca sexta serpinome: Analysis of serpin genes and proteins in the tobacco hornworm

Christen

Dittmer

et al. 2018

Insect Biochemistry and Molecular Biology

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Members of the serpin superfamily of proteins occur in animals, plants, bacteria, archaea and some viruses. They adopt a variety of physiological functions, including regulation of immune system, modulation of apoptosis, hormone transport and acting as storage proteins. Most members of the serpin family are inhibitors of serine proteinases. In this study, we searched the genome of Manduca sexta and identified 32 serpin genes. We analyzed the structure of these genes and the sequences of their encoded proteins. Three M. sexta genes (serpin-1, serpin-15, and serpin-28) have mutually exclusive alternatively spliced exons encoding the carboxyl-terminal reactive center loop of the protein, which is the site of interaction with target proteases. We discovered that MsSerpin-1 has 14 splicing isoforms, including two undiscovered in previous studies. Twenty-eight of the 32 M. sexta serpins include a putative secretion signal peptide and are predicted to be extracellular proteins. Phylogenetic analysis of serpins in M. sexta and Bombyx mori indicates that 17 are orthologous pairs, perhaps carrying out essential physiological functions. Analysis of the reactive center loop and hinge regions of the protein sequences indicates that 16 of the serpin genes encode proteins that may lack proteinase inhibitor activity. Our annotation and analysis of these serpin genes and their transcript profiles should lead to future advances in experimental study of their functions in insect biochemistry.

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Section: Resultsmentioning

confidence: 99%

The Manduca sexta serpinome: Analysis of serpin genes and proteins in the tobacco hornworm

Christen

Dittmer

et al. 2018

Insect Biochemistry and Molecular Biology

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“…1C) [21, 29, 59]. These properties are present in the earlier described serpin-like structures, such as antitrypsin (PDB: 7API) [18], ovalbumin (PDB: 1OVA) [90], antichymotrypsin (PDB: 2ACH) [6], and plasminogen activator 1(PAI1) (PDB: 1C5G) [66], as well as in the more recently described ones, such as serpin18 (PDB: 4R9I) [23], SRPN18 (PDB: 5C98) [63], and vaspin (PDB: 4IF8) [26].…”

Section: Discussionmentioning

confidence: 99%

Identification and partial characterization of a novel serpin fromEudiplozoon nipponicum(Monogenea, Polyopisthocotylea)

et al. 2018

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Background: Serpins are a superfamily of serine peptidase inhibitors that participate in the regulation of many physiological and cell peptidase-mediated processes in all organisms (e.g. in blood clotting, complement activation, fibrinolysis, inflammation, and programmed cell death). It was postulated that in the blood-feeding members of the monogenean family Diplozoidae, serpins could play an important role in the prevention of thrombus formation, activation of complement, inflammation in the host, and/or in the endogenous regulation of protein degradation. Results: In silico analysis showed that the DNA and primary protein structures of serpin from Eudiplozoon nipponicum (EnSerp1) are similar to other members of the serpin superfamily. The inhibitory potential of EnSerp1 on four physiologically-relevant serine peptidases (trypsin, factor Xa, kallikrein, and plasmin) was demonstrated and its presence in the worm’s excretory-secretory products (ESPs) was confirmed. Conclusion: EnSerp1 influences the activity of peptidases that play a role in blood coagulation, fibrinolysis, and complement activation. This inhibitory potential, together with the serpin’s presence in ESPs, suggests that it is likely involved in host-parasite interactions and could be one of the molecules involved in the control of feeding and prevention of inflammatory responses.

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“…4 Scott Lovell (University of Kansas, USA) detailed the importance of structural biology approaches for the advancement of chemical biology with some illustrative examples. 5 Finally, Andrew Zhang (AstraZeneca, USA) closed the session sharing his experience in industry and detailing the increased importance of chemical biology approaches and directions being taken in Big Pharmaceutical companies. 6 Overall, the session covered a wide range of technologies and provided useful advice for both young and seasoned chemical biologists.…”

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confidence: 99%