Biology:Calponin
| Calponin Homology Domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 CH domain from H.Sapiends Calponin 1. PDB 1wyp | |||||||||
| Identifiers | |||||||||
| Symbol | CH | ||||||||
| Pfam | PF00307 | ||||||||
| Pfam clan | CL0188 | ||||||||
| InterPro | IPR001715 | ||||||||
| |||||||||
| calponin 1, basic, smooth muscle | |
|---|---|
Solution structure of the CH domain of human Calponin 1. Rainbow colored cartoon (N-terminus = blue, C-terminus = red).[1] | |
| Identifiers | |
| Symbol | CNN1 |
| NCBI gene | 1264 |
| HGNC | 2155 |
| OMIM | 600806 |
| PDB | 1WYP |
| RefSeq | NM_001299 |
| UniProt | P51911 |
| Other data | |
| Locus | Chr. 19 p13.2-13.1 |
| calponin 2 | |
|---|---|
| Identifiers | |
| Symbol | CNN2 |
| NCBI gene | 1265 |
| HGNC | 2156 |
| OMIM | 602373 |
| RefSeq | NM_004368 |
| UniProt | Q99439 |
| Other data | |
| Locus | Chr. 19 p13.3 |
| calponin 3, acidic | |
|---|---|
| Identifiers | |
| Symbol | CNN3 |
| NCBI gene | 1266 |
| HGNC | 2157 |
| OMIM | 602374 |
| RefSeq | NM_001839 |
| UniProt | Q6FHA7 |
| Other data | |
| Locus | Chr. 1 p22-p21 |
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.
Structure and function
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]
References
- ↑ PDB: 1WYP; RCSB PDB - 1WYP Structure Summary. RCSB Protein Data Bank. doi:10.2210/pdb1wyp/pdb. http://www.pdb.org/pdb/explore/explore.do?structureId=1WYP.
- ↑ 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. http://www.bms.ed.ac.uk/research/others/smaciver/Cyto-Topics/Calponin_Family.htm.
External links
- Calponin at the US National Library of Medicine Medical Subject Headings (MeSH)
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