serpin B11
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Function
- no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change
Structure
belongs to the serpin family, Ov-serpin subfamily
Compartment
Alternative splicing
named isoforms=3
Expression
Pathology
- mutations in the scaffold leading to either a stop codon instead of a Glu at position 90, an Arg instead of the well conserved Trp at position 188, or a Pro instead of Ser at position 303 lead to the loss of inhibitory activity
Polymorphism
according to some authors,
- 4 of the identified SERPIN11 transcripts contain coding sequences distinguished by different combinations of single nucleotide polymorphisms (SERPINB11a, SERPINB11b, SERPINB11c, & SERPINB11d), & one contained
- a nonsense mutation introduces a premature stop codon in position 90 (SERPINB11f)[2]
More general terms
References
- ↑ UniProt http://www.uniprot.org/uniprot/Q96P15.html
- ↑ 2.0 2.1 Askew DJ et al SERPINB11 is a new noninhibitory intracellular serpin. Common single nucleotide polymorphisms in the scaffold impair conformational change. J Biol Chem. 2007 Aug 24;282(34):24948-60. Epub 2007 Jun 11 PMID: https://www.ncbi.nlm.nih.gov/pubmed/17562709