Calponin is a calcium binding protein. Calponin tonically inhibits the ATPase activity of myosin in smooth muscle. Phosphorylation of calponin by a protein kinase, which is dependent upon calcium binding to calmodulin, releases the calponin's inhibition of the smooth muscle ATPase.
Calponin is mainly made up of α-helices with hydrogen bond turns. It is a binding protein and is made up of three domains. These domains in order of appearance are Calponin Homology (CH), regulatory domain (RD), and Click-23, domain that contains the calponin repeats. At the CH domain calponin binds to α-actin and filamin and binds to actin within the RD domain. Calmodulin, when activated by calcium may bind weakly to the CH domain and inhibit calponin binding with α-actin.[2] Calponin is responsible for binding many actin binding proteins, phospholipids, and regulates the actin/myosin interaction. Calponin is also thought to negatively affect the bone making process due to being expressed in high amounts in osteoblasts.[3]
^PDB: 1WYP; Tomizawa T, Kigawa T, Koshiba S, Inoue M, Yokoyama S. "RCSB PDB - 1WYP Structure Summary". RCSB Protein Data Bank. doi:10.2210/pdb1wyp/pdb. {{cite journal}}: Cite journal requires |journal= (help)
^Ferjani, I; Fattoum, A; Manai, M; Benyamin, Y; Roustan, C; Maciver, SK (September 2010). "Two distinct regions of calponin share common binding sites on actin resulting in different modes of calponin-actin interaction". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1804 (9): 1760–7. doi:10.1016/j.bbapap.2010.05.012. PMID 20595006.
^Maciver S. "The Calponin Family". Department of Biomedical Sciences, University of Edinburgh. Retrieved 2011-04-25.
calponin, calcium, binding, protein, tonically, inhibits, atpase, activity, myosin, smooth, muscle, phosphorylation, calponin, protein, kinase, which, dependent, upon, calcium, binding, calmodulin, releases, calponin, inhibition, smooth, muscle, atpase, homolo. Calponin is a calcium binding protein Calponin tonically inhibits the ATPase activity of myosin in smooth muscle Phosphorylation of calponin by a protein kinase which is dependent upon calcium binding to calmodulin releases the calponin s inhibition of the smooth muscle ATPase Calponin Homology DomainCH domain from H Sapiends Calponin 1 PDB 1wypIdentifiersSymbolCHPfamPF00307Pfam clanCL0188InterProIPR001715Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summarycalponin 1 basic smooth muscleSolution structure of the CH domain of human Calponin 1 Rainbow colored cartoon N terminus blue C terminus red 1 IdentifiersSymbolCNN1NCBI gene1264HGNC2155OMIM600806PDB1WYPRefSeqNM 001299UniProtP51911Other dataLocusChr 19 p13 2 13 1Search forStructuresSwiss modelDomainsInterProcalponin 2IdentifiersSymbolCNN2NCBI gene1265HGNC2156OMIM602373RefSeqNM 004368UniProtQ99439Other dataLocusChr 19 p13 3Search forStructuresSwiss modelDomainsInterProcalponin 3 acidicIdentifiersSymbolCNN3NCBI gene1266HGNC2157OMIM602374RefSeqNM 001839UniProtQ6FHA7Other dataLocusChr 1 p22 p21Search forStructuresSwiss modelDomainsInterProStructure and function EditCalponin is mainly made up of a helices with hydrogen bond turns It is a binding protein and is made up of three domains These domains in order of appearance are Calponin Homology CH regulatory domain RD and Click 23 domain that contains the calponin repeats At the CH domain calponin binds to a actin and filamin and binds to actin within the RD domain Calmodulin when activated by calcium may bind weakly to the CH domain and inhibit calponin binding with a actin 2 Calponin is responsible for binding many actin binding proteins phospholipids and regulates the actin myosin interaction Calponin is also thought to negatively affect the bone making process due to being expressed in high amounts in osteoblasts 3 nbsp Immunohistochemistry for calponin in ductal carcinoma in situ highlighting myoepithelial cells around all tumor cells thereby ruling out invasive ductal carcinoma References Edit PDB 1WYP Tomizawa T Kigawa T Koshiba S Inoue M Yokoyama S RCSB PDB 1WYP Structure Summary RCSB Protein Data Bank doi 10 2210 pdb1wyp pdb a href Template Cite journal html title Template Cite journal cite journal a Cite journal requires journal help Ferjani I Fattoum A Manai M Benyamin Y Roustan C Maciver SK September 2010 Two distinct regions of calponin share common binding sites on actin resulting in different modes of calponin actin interaction Biochimica et Biophysica Acta BBA Proteins and Proteomics 1804 9 1760 7 doi 10 1016 j bbapap 2010 05 012 PMID 20595006 Maciver S The Calponin Family Department of Biomedical Sciences University of Edinburgh Retrieved 2011 04 25 External links EditCalponin at the U S National Library of Medicine Medical Subject Headings MeSH nbsp This protein related article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Calponin amp oldid 1113356840, wikipedia, wiki, book, books, library,
