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Šaperon (protein)

Pogled od gore na model GroES/GroEL bakterijskog šaperonskog kompleksa

Šaperoni su posebni proteinski molekuli, poznati i kao molekularni pratioci, koji pomažu u savijanju i uvijanju polipeptidnog lanca proteina, dovodeći ga u stabilnu konformaciju.[1][2] Učestvuju u postizanju potrebne trodimenzionalne strukture za delovanje proteina.[3] Izuzetno su značajni u situacijama stresa, kao što je povišena temperatura, pri čemu održavaju strukturu proteina u potrebnom obliku, i sprečavaju proteinsku denaturaciju. Zbog ovog svojstva mnogi, ali svakako ne svi, šaperoni spadaju u tzv. HSP proteine (engl. Heat shock proteins), tj. 'proteine toplotnog udara'. Neki šaperoni nose specifičnu informaciju o uvijanju proteina u trodimenzionalne strukture, bez koje takvi proteini ne mogu biti formirani. Takvi proteini krše Anfinsenovu hipotezu,[4] i ne mogu se spontano organizovati.

  1. ^ Richardson, RT; Alekseev, OM; Grossman, G; et al. (2006). „Nuclear Autoantigenic Sperm Protein (NASP), a Linker Histone Chaperone That is Required for Cell Proliferation”. Journal of Biological Chemistry. 281 (30): 21526—34. PMID 16728391. doi:10.1074/jbc.M603816200. 
  2. ^ Alekseev OM, Richardson RT, Alekseev O, O'Rand MG (2009). „Analysis of gene expression profiles in HeLa cells in response to overexpression or siRNA-mediated depletion of NASP”. Reproductive Biology and Endocrinology. 7: 45. PMC 2686705Слободан приступ. PMID 19439102. doi:10.1186/1477-7827-7-45. 
  3. ^ Ellis, RJ (2006). „Molecular chaperones: assisting assembly in addition to folding”. Trends in Biochemical Sciences. 31 (7): 395—401. PMID 16716593. doi:10.1016/j.tibs.2006.05.001. 
  4. ^ Kris Pauwels and other (2007). „Chaperoning Anfinsen:The Steric Foldases” (PDF). Molecular Microbiology. 64 (4): 917. doi:10.1111/j.1365-2958.2007.05718.x. Архивирано из оригинала (PDF) 23. 05. 2012. г. 
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Šaperon (protein)
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