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Genomics, evolution and biological functions of the pacifastin peptide family: a conserved serine protease inhibitor family in arthropods
- Source :
- Peptides. 24:1633-1644
- Publication Year :
- 2003
- Publisher :
- Elsevier BV, 2003.
-
Abstract
- The last decade, a new serine protease inhibitor family has been described in arthropods. Eight members were purified from the locusts Locusta migratoria (LMPI-1-2 and HI) and Schistocerca gregaria (SGPI-1-5). The light chain of the heterodimeric protease inhibitor pacifastin, from the freshwater crayfish Pacifastacus leniusculus, was found to be composed of nine consecutive inhibitory domains (PLDs). These domains share a pattern of six conserved cysteine residues (Cys-Xaa(9-12)-Cys-Asn-Xaa-Cys-Xaa-Cys-Xaa(2-3)-Gly-Xaa(3-6)-Cys-Thr-Xaa(3)-Cys) with the locust inhibitors. Via cDNA cloning, eight pacifastin-related precursors have been identified in locusts. Interestingly, additional pacifastin-related precursors have been identified in Diptera, Lepidoptera and Coleoptera utilising an in silico data mining approach.
- Subjects :
- Serine Proteinase Inhibitors
animal structures
Physiology
Molecular Sequence Data
Biochemistry
Conserved sequence
Evolution, Molecular
Cellular and Molecular Neuroscience
Endocrinology
medicine
Animals
Amino Acid Sequence
Pacifastin
Arthropods
Peptide sequence
Conserved Sequence
Serine protease
Base Sequence
biology
Proteins
Genomics
biology.organism_classification
Protease inhibitor (biology)
body regions
biology.protein
Schistocerca
Locust
medicine.drug
Subjects
Details
- ISSN :
- 01969781
- Volume :
- 24
- Database :
- OpenAIRE
- Journal :
- Peptides
- Accession number :
- edsair.doi.dedup.....dfdccf6c24c9286f651a7ef954f510b4