cd19956

serpin B family, ov-serpins

CDD entry
Member databaseCDD
CDD typedomain
Short nameserpinB
Setserpin

Description

The clade B of the serpin superfamily corresponds to the ovalbumin family of serpins (ov-serpins), a family of closely related proteins, whose members can be secreted (ovalbumin), cytosolic (leukocyte elastase inhibitor, LEI), or targeted to both compartments (plasminogen activator inhibitor 2, PAI-2). Family members are also characterized by N- and C-terminal extensions, the absence of a signal peptide, and a Ser rather than an Asn residue at the penultimate position. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants can cause blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.
[8, 7, 11, 6, 4, 5, 9, 10, 3, 2, 1]

References

1.Serpin structure, mechanism, and function. Gettins PG. Chem. Rev. 102, 4751-804, (2002). View articlePMID: 12475206

2.Phylogeny of the serpin superfamily: implications of patterns of amino acid conservation for structure and function. Irving JA, Pike RN, Lesk AM, Whisstock JC. Genome Res. 10, 1845-64, (2000). View articlePMID: 11116082

3.The serpins: evolution and adaptation in a family of protease inhibitors. Carrell RW, Pemberton PA, Boswell DR. Cold Spring Harb. Symp. Quant. Biol. 52, 527-35, (1987). PMID: 3502621

4.Maspin, a serpin with tumor-suppressing activity in human mammary epithelial cells. Zou Z, Anisowicz A, Hendrix MJ, Thor A, Neveu M, Sheng S, Rafidi K, Seftor E, Sager R. Science 263, 526-9, (1994). View articlePMID: 8290962

5.The ovalbumin family of serpin proteins. Remold-O'Donnell E. FEBS Lett. 315, 105-8, (1993). View articlePMID: 8417965

6.Inhibition of interleukin-1 beta converting enzyme by the cowpox virus serpin CrmA. An example of cross-class inhibition. Komiyama T, Ray CA, Pickup DJ, Howard AD, Thornberry NA, Peterson EP, Salvesen G. J. Biol. Chem. 269, 19331-7, (1994). View articlePMID: 8034697

7.Neuroserpin, an axonally secreted serine protease inhibitor. Osterwalder T, Contartese J, Stoeckli ET, Kuhn TB, Sonderegger P. EMBO J. 15, 2944-53, (1996). View articlePMID: 8670795

8.The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature. Silverman GA, Bird PI, Carrell RW, Church FC, Coughlin PB, Gettins PG, Irving JA, Lomas DA, Luke CJ, Moyer RW, Pemberton PA, Remold-O'Donnell E, Salvesen GS, Travis J, Whisstock JC. J. Biol. Chem. 276, 33293-6, (2001). View articlePMID: 11435447

9.Pigment epithelium-derived factor: neurotrophic activity and identification as a member of the serine protease inhibitor gene family. Steele FR, Chader GJ, Johnson LV, Tombran-Tink J. Proc. Natl. Acad. Sci. U.S.A. 90, 1526-30, (1993). View articlePMID: 8434014

10.Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins. Huber R, Carrell RW. Biochemistry 28, 8951-66, (1989). View articlePMID: 2690952

11.Crystallography of serpins and serpin complexes. Dunstone MA, Whisstock JC. Methods Enzymol 501, 63-87, (2011). PMID: 22078531

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