Summary: Arthropod defensin
This is the Wikipedia entry entitled "Arthropod defensin". More...
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Arthropod defensin Edit Wikipedia article
|Structure of insect defensin A.|
Arthropod defensins are a family of insect and scorpion cysteine-rich antibacterial peptides, primarily active against Gram-positive bacteria. All these peptides range in length from 38 to 51 amino acids. There are six conserved cysteines all involved in intrachain disulfide bonds.
A schematic representation of peptides from the arthropod defensin family is shown below.
+----------------------------+ | | xxCxxxxxxxxxxxxxxCxxxCxxxxxxxxxCxxxxxCxCxx | | | | +---|---------------+ | +-----------------+
'C': conserved cysteine involved in a disulfide bond.
Although low level sequence similarities have been reported between the arthropod defensins and mammalian defensins, the topological arrangement of the disulfide bonds as well as the tertiary structure are completely different in the two families.
- Cornet B, Bonmatin JM, Hetru C, Hoffmann JA, Ptak M, Vovelle F (May 1995). "Refined three-dimensional solution structure of insect defensin A". Structure 3 (5): 435–48. DOI:10.1016/S0969-2126(01)00177-0. PMID 7663941.
- Dunbar B, Lambert J, Keppi E, Wicker C, Lepage P, Hoffmann J, Fothergill J, Dimarcq JL, Reichhart JM, Van Dorsselaer A (1989). "Insect immunity: isolation from immune blood of the dipteran Phormia terranovae of two insect antibacterial peptides with sequence homology to rabbit lung macrophage bactericidal peptides". Proc. Natl. Acad. Sci. U.S.A. 86 (1): 262–266. DOI:10.1073/pnas.86.1.262. PMC 286444. PMID 2911573. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=286444.
- Kobayashi K, Fujiwara S, Imai J, Fujiwara M, Yaeshima T, Kawashima T (1990). "A potent antibacterial protein in royal jelly. Purification and determination of the primary structure of royalisin". J. Biol. Chem. 265 (19): 11333–11337. PMID 2358464.
- Yamada K, Natori S (1993). "Purification, sequence and antibacterial activity of two novel sapecin homologues from Sarcophaga embryonic cells: similarity of sapecin B to charybdotoxin". Biochem. J. 291: 275–279. PMC 1132513. PMID 8471044. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1132513.
- Cociancich S, Bulet P, Hoffmann JA, Hetru C, Lambert J, Hoffmann D, Dimarcq JL, Reichhart JM (1991). "Insect immunity. Isolation from a coleopteran insect of a novel inducible antibacterial peptide and of new members of the insect defensin family". J. Biol. Chem. 266 (36): 24520–24525. PMID 1761552.
- Cociancich S, Bulet P, Hoffmann JA, Hegy G, Hetru C, Reuland M, Sauber F, Bischoff R, Van Dorsselaer A (1992). "A novel insect defensin mediates the inducible antibacterial activity in larvae of the dragonfly Aeschna cyanea (Paleoptera, Odonata)". Eur. J. Biochem. 209 (3): 977–984. DOI:10.1111/j.1432-1033.1992.tb17371.x. PMID 1425705.
- Natori S, Kohda D, Hanzawa H, Shimada I, Kuzuhara T, Komano H, Inagaki F, Arata Y (1990). "1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin". FEBS Lett. 269 (2): 413–420. DOI:10.1016/0014-5793(90)81206-4. PMID 2401368.
 Further reading
- This article incorporates text from the public domain Pfam and InterPro IPR001542
- PDOC00356 - Arthropod defensins in PROSITE (=source of figure)
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External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001542
Arthropod defensins are a family of insect and scorpion cysteine-rich antibacterial peptides, primarily active against Gram-positive bacteria [PUBMED:2911573, PUBMED:2358464, PUBMED:8471044, PUBMED:1761552, PUBMED:1425705]. All these peptides range in length from 38 to 51 amino acids. There are six conserved cysteines all involved in intrachain disulphide bonds.
A schematic representation of peptides from the arthropod defensin family is shown below.
+----------------------------+ | | xxCxxxxxxxxxxxxxxCxxxCxxxxxxxxxCxxxxxCxCxx | | | | +---|---------------+ | +-----------------+ 'C': conserved cysteine involved in a disulphide bond.
Although low level sequence similarities have been reported [PUBMED:2911573] between the arthropod defensins and mammalian defensins, the topological arrangement of the disulphide bonds as well as the tertiary structure [PUBMED:2401368] are completely different in the two families.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Biological process||defense response (GO:0006952)|
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Curation and family details
|Previous IDs:||Defensin; Arthro_defensin;|
|Author:||Finn RD, Bateman A|
|Number in seed:||15|
|Number in full:||314|
|Average length of the domain:||33.90 aa|
|Average identity of full alignment:||42 %|
|Average coverage of the sequence by the domain:||40.60 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Defensin_2 domain has been found. There are 14 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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