Biology:Trappin protein transglutaminase binding domain
| Cementoin | |||||||||
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 solution structure of r-elafin, a specific inhibitor of elastase, nmr, 11 structures | |||||||||
| Identifiers | |||||||||
| Symbol | Cementoin | ||||||||
| Pfam | PF10511 | ||||||||
| InterPro | IPR019541 | ||||||||
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In molecular biology, the trappin protein transglutaminase binding domain or cementoin is a protein domain found at the N-terminus of Whey Acidic Protein (WAP) domain-containing protease inhibitors such as trappin-2. This N-terminal domain enables it to become cross-linked to extracellular matrix proteins by transglutaminase.[1] This domain contains several repeated motifs with the consensus sequence Gly-Gln-Asp-Pro-Val-Lys, and these together can anchor the whole molecule to extracellular matrix proteins, such as laminin, fibronectin, beta-crystallin, collagen IV, fibrinogen, and elastin, by transglutaminase-catalysed cross-links. The whole domain is rich in glutamine and lysine, thus allowing transglutaminase(s) to catalyse the formation of an intermolecular epsilon-(gamma-glutamyl)lysine isopeptide bond.[2]
References
- ↑ "The trappin gene family: proteins defined by an N-terminal transglutaminase substrate domain and a C-terminal four-disulphide core". Biochem. J. 340 (3): 569–77. June 1999. doi:10.1042/0264-6021:3400569. PMID 10359639.
- ↑ "Multifaceted roles of human elafin and secretory leukocyte proteinase inhibitor (SLPI), two serine protease inhibitors of the chelonianin family". Biochimie 90 (2): 284–95. February 2008. doi:10.1016/j.biochi.2007.09.007. PMID 17964057.
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