REVIEW: Peptidyl-Prolyl cis-trans Isomerases: Structure and Functions

B. K. Pliyev¹ and B. Ya. Gurvits^2*

¹Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow, 117871 Russia; fax: (095) 330-6538; E-mail: dvor@humgen.siobc.ras.ru

²Bach Institute of Biochemistry, Russian Academy of Sciences, Leninskii pr. 33, Moscow, 117071 Russia; fax: (095) 954-2732; E-mail: inbio@glas.apc.org

^* To whom correspondence should be addressed.

Received November 11, 1998; Revision received March 23, 1999

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Peptidyl-prolyl cis-trans isomerases (PPI) catalyze cis-trans isomerization of imide bonds in peptides and proteins. This review summarizes the literature on the structure and functions of PPIs, their involvement in protein folding, and organization of PPI-containing receptors and membrane channels. A possible role of several PPIs in distant interactions between cells is discussed.

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KEY WORDS: peptidyl-prolyl cis-trans isomerase, folding, catalysis mechanisms, multifunctionality, chaperones, immunophilins

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