Small protein with high number of disulphide bonds
Cysteine-rich proteins (CRP, cysteine-rich peptide or disulphide-rich peptide) are small proteins that contain a large number of cysteines. These cysteines either cross-link to form disulphide bonds, or bind metal ions by chelation, stabilising the protein's tertiary structure.[1][2][3] CRPs include a highly conserved secretion peptide signal at the N-terminus and a cysteine-rich region at the C-terminus.[4]
- ^ Cheek S, Krishna SS, Grishin NV (May 2006). "Structural classification of small, disulfide-rich protein domains". Journal of Molecular Biology. 359 (1): 215–37. doi:10.1016/j.jmb.2006.03.017. PMID 16618491.
- ^ Arolas JL, Aviles FX, Chang JY, Ventura S (May 2006). "Folding of small disulfide-rich proteins: clarifying the puzzle". Trends in Biochemical Sciences. 31 (5): 292–301. doi:10.1016/j.tibs.2006.03.005. PMID 16600598. S2CID 30709875.
- ^ Metallothioneins and related chelators. Sigel, Astrid., Sigel, Helmut., Sigel, Roland K. O. Cambridge: Royal Society of Chemistry. 2009. ISBN 978-1-84755-953-1. OCLC 429670531.
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- ^ Marshall E, Costa LM, Gutierrez-Marcos J (March 2011). "Cysteine-rich peptides (CRPs) mediate diverse aspects of cell-cell communication in plant reproduction and development". Journal of Experimental Botany. 62 (5): 1677–86. doi:10.1093/jxb/err002. PMID 21317212.