prefoldin Antikörper

Molecular chaperones are proteins that assist in the correct folding of other proteins in the crowded molecular environment that exists in living cells (1). Within this class of proteins, a key role is played by chaperonins, multisubunit toroidal (i.e. doughnut-shaped) assemblies that undergo major ATP-dependent conformational changes as part of the mechanism of facilitated folding. Prefoldin is a heterohexameric chaperone protein which has the ability to capture unfolded Actin. Six prefoldin polypeptides, prefoldin 1-prefoldin 6, have been identified. Prefoldin 1 is a 122 amino acid protein that binds specifically to cytosolic chaperonin (c-cpn) and transfers target proteins to it. Prefoldin 3 (VBP1 or VHL binding protein-1) forms complexes with VHL and is translocated from perinuclear granules to the nucleus or cytoplasm. Prefoldin 4 is a possible transcription factor. Prefoldin 5 (c-Myc-binding protein Mm-1, Myc modulator 1 or MM-1) is a c-Myc binding protein.