Crystal structure of the post-chaperonin beta-tubulin binding cofactor Rbl2p.

摘要: The folding pathway of tubulins includes highly specific interactions with a series cofactors (A, B, C, D and E) after they are released from the eukaryotic chaperonin CCT. 2.2 A crystal structure Rbl2p, Saccharomyces cerevisiae homolog beta-tubulin cofactor A, shows alpha-helical monomers forming flat, slightly convex dimer. surface molecule is dominated by polar charged residues lacks hydrophobic patches typically observed for chaperones that bind unfolded or partially folded proteins. This post-chaperonin therefore clearly distinct typical where hydrophobicity hallmark substrate recognition.