Biology:SERPINB10
 Generic protein structure example |
Serpin peptidase inhibitor, clade B (ovalbumin), member 10 is a protein that in humans is encoded by the SERPINB10 gene.[1]
Function
The superfamily of high molecular weight serine proteinase inhibitors (serpins) regulate a diverse set of intracellular and extracellular processes such as complement activation, fibrinolysis, coagulation, cellular differentiation, tumor suppression, apoptosis, and cell migration. Serpins are characterized by a well-conserved tertiary structure that consists of 3 beta sheets and 8 or 9 alpha helices.[2] A critical portion of the molecule, the reactive center loop connects beta sheets A and C. Protease inhibitor-10 (PI10; SERPINB10) is a member of the ov-serpin subfamily, which, relative to the archetypal serpin PI1, is characterized by a high degree of homology to chicken ovalbumin, lack of N- and C-terminal extensions, absence of a signal peptide, and a serine rather than an asparagine residue at the penultimate position.[3]
References
- ↑ "Entrez Gene: Serpin peptidase inhibitor, clade B (ovalbumin), member 10". https://www.ncbi.nlm.nih.gov/gene/5273.
- ↑ "Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins". Biochemistry 28 (23): 8951–66. November 1989. doi:10.1021/bi00449a001. PMID 2690952.
- ↑ * "Cytoplasmic antiproteinase 2 (PI8) and bomapin (PI10) map to the serpin cluster at 18q21.3". Genomics 43 (3): 321–8. August 1997. doi:10.1006/geno.1997.4827. PMID 9268635.
Further reading
- "Identification of a nuclear targeting domain in the insertion between helices C and D in protease inhibitor-10". The Journal of Biological Chemistry 274 (16): 11194–8. April 1999. doi:10.1074/jbc.274.16.11194. PMID 10196205.
- "Novel pancreatic beta cell-specific proteins: antibody-based proteomics for identification of new biomarker candidates". Journal of Proteomics 75 (9): 2611–20. May 2012. doi:10.1016/j.jprot.2012.03.008. PMID 22465717.
- "Protease inhibitor 10 inhibits tumor necrosis factor alpha -induced cell death. Evidence for the formation of intracellular high M(r) protease inhibitor 10-containing complexes". The Journal of Biological Chemistry 275 (34): 26385–9. August 2000. doi:10.1074/jbc.C000389200. PMID 10871600.
- "Bomapin is a redox-sensitive nuclear serpin that affects responsiveness of myeloid progenitor cells to growth environment". BMC Cell Biology 11: 30. April 2010. doi:10.1186/1471-2121-11-30. PMID 20433722.
- "Nucleotide variations in genes encoding plasminogen activator inhibitor-2 and serine proteinase inhibitor B10 associated with prostate cancer". Journal of Human Genetics 50 (10): 507–15. 2005. doi:10.1007/s10038-005-0285-1. PMID 16172807.
- "Molecular cloning of bomapin (protease inhibitor 10), a novel human serpin that is expressed specifically in the bone marrow". The Journal of Biological Chemistry 270 (45): 26754–7. November 1995. doi:10.1074/jbc.270.45.26754. PMID 7592909.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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