A conserved folding mechanism for PDZ domains.
An important question in protein folding is whether the folding mechanism is sequence dependent and conserved for homologous proteins. In this work we compared the kinetic folding mechanism of five postsynaptic density protein-95, disc-large tumor suppressor protein, zonula occludens-1 (PDZ) domains, sharing similar topology but having different primary structures. Investigation of the different proteins under various experimental conditions revealed that the folding kinetics of each member of the PDZ family can be described by a model with two transition states separated by an intermediate. Moreover, the positions of the two transition states along the reaction coordinate (as given by their beta(T)-values) are fairly constant for the five PDZ domains.
Chi
Celestine N
CN
Department of Medical Biochemistry and Microbiology, Uppsala University, BMC Box 582, SE-75123 Uppsala, Sweden.
Gianni
Stefano
S
Calosci
Nicoletta
N
Travaglini-Allocatelli
Carlo
C
Engström
Ke
K
Jemth
Per
P
D000076122:Disks Large Homolog 4 Protein; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins / Q000737:chemistry*; D007700:Kinetics; D008565:Membrane Proteins / Q000737:chemistry*; D017510:Protein Folding; D020673:Protein Renaturation; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D040681:Structural Homology, Protein; D013816:Thermodynamics; D019108:Tight Junctions / Q000737:chemistry*
C501444:DLG4 protein, human; D000076122:Disks Large Homolog 4 Protein; D047908:Intracellular Signaling Peptides and Proteins; D008565:Membrane Proteins