Polypeptide binding proteins: what remains to be discovered?
Many proteins have developed the potential to sequester a client polypeptide chain in its various folding states as a specific intermolecular ligand and, thus, exhibit the properties of a holding chaperone. The resulting complexes can be of a diverse nature in terms of structure and reaction dynamics and are characterized on the basis of various microscopic properties including formation and decay of encounter and Michaelis complexes as well as reactant and product stability. Interpretation of the functional consequences of complex formation in the cell generally tends to be rather complicated, with notable exceptions including complexes formed during the reaction pathways of proteases, protein kinases and protein phosphatases. Peptide bond cis/trans isomerases take up an intermediate position among the poly(oligo)peptide binding proteins because, although the relationship between chain sequestration and catalysis of isomerization can easily be delineated in vitro, it is sometimes difficult to resolve in the cell. Time-resolved studies on interactions involving peptide bond cis/trans isomerases have led to the establishment of generally applicable methods for studying protein-poly(oligo)peptide interactions that are capable of identifying new types of biocatalysis.
Fischer
Gunter
G
Max-Planck Research Unit for Enzymology of Protein Folding, Max Planck Society, Weinbergweg 22, D-06120 Halle/Saale, Germany. fischer@enzyme-halle.mpg.de
Wawra
Stephan
S
D002352:Carrier Proteins; D007535:Isomerases / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D025941:Protein Interaction Mapping / Q000379:methods*; D011506:Proteins / Q000737:chemistry*
D002352:Carrier Proteins; D010455:Peptides; D011506:Proteins; D007535:Isomerases