Biology:Clp protease family
| CLP_protease | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of the clpp protease catalytic domain from plasmodium falciparum | |||||||||
| Identifiers | |||||||||
| Symbol | CLP_protease | ||||||||
| Pfam | PF00574 | ||||||||
| Pfam clan | CL0127 | ||||||||
| InterPro | IPR001907 | ||||||||
| PROSITE | PDOC00358 | ||||||||
| MEROPS | S14 | ||||||||
| SCOP2 | 1tyf / SCOPe / SUPFAM | ||||||||
| CDD | cd00394 | ||||||||
| |||||||||
In molecular biology, the CLP protease family is a family of serine peptidases belong to the MEROPS peptidase family S14 (ClpP endopeptidase family, clan SK). ClpP is an ATP-dependent protease that cleaves a number of proteins, such as casein and albumin.[1] It exists as a heterodimer of ATP-binding regulatory A and catalytic P subunits, both of which are required for effective levels of protease activity in the presence of ATP,[1] although the P subunit alone does possess some catalytic activity.
Proteases highly similar to ClpP have been found to be encoded in the genome of bacteria, in the mitochondria of metazoa, some viruses and in the chloroplast of plants. A number of the proteins in this family are classified as non-peptidase homologues as they have been found experimentally to be without peptidase activity, or lack amino acid residues that are believed to be essential for catalytic activity.
Mutations in mitochondrial CLPP are associated with Perrault syndrome[2][3][4][5] and cause a variety of molecular defects, from the loss of ATPase docking, to the activation or inhibition of peptidase activity.[3][6]
See also
References
- ↑ 1.0 1.1 "Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli". The Journal of Biological Chemistry 265 (21): 12536–45. July 1990. doi:10.1016/S0021-9258(19)38378-4. PMID 2197275.
- ↑ Newman, W. G.; Friedman, T. B.; Conway, G. S.; Demain LAM; Adam, M. P.; Ardinger, H. H.; Pagon, R. A.; Wallace, S. E. et al. (1993). Adam, Margaret P.; Ardinger, Holly H.; Pagon, Roberta A. et al.. eds. "Perrault Syndrome". GeneReviews (Seattle (WA): University of Washington, Seattle). PMID 25254289. http://www.ncbi.nlm.nih.gov/books/NBK242617/. Retrieved 2020-11-18.
- ↑ 3.0 3.1 "Perrault syndrome is caused by recessive mutations in CLPP, encoding a mitochondrial ATP-dependent chambered protease". American Journal of Human Genetics 92 (4): 605–13. April 2013. doi:10.1016/j.ajhg.2013.02.013. PMID 23541340.
- ↑ "Exome analysis identified a novel missense mutation in the CLPP gene in a consanguineous Saudi family expanding the clinical spectrum of Perrault Syndrome type-3". Journal of the Neurological Sciences 353 (1–2): 149–54. June 2015. doi:10.1016/j.jns.2015.04.038. PMID 25956234.
- ↑ "A Novel Missense Mutation in the CLPP Gene Causing Perrault Syndrome Type 3 in a Turkish Family". Journal of Clinical Research in Pediatric Endocrinology 8 (4): 472–477. December 2016. doi:10.4274/jcrpe.2717. PMID 27087618.
- ↑ "Perrault syndrome type 3 caused by diverse molecular defects in CLPP". Scientific Reports 8 (1): 12862. August 2018. doi:10.1038/s41598-018-30311-1. PMID 30150665. Bibcode: 2018NatSR...812862B.
External links
 |  |
