Structural and thermodynamic characterization of the self-adhesive properties of human P-cadherin.
Human P-cadherin is a promising therapeutic target against cancer. However, its characterization at the molecular level is still lacking. We report that human P-cadherin associated irreversibly in a distinct dimer configuration. Unexpectedly, the divalent cation Ca²⁺ was not necessary for dimerization, although it greatly stabilized the protein-protein complex.
Department of Medical Genome Sciences, The University of Tokyo, Tokyo 108-8639, Japan.
Shota
S
Kudo
Jose M M
JM
Caaveiro
Takamitsu
T
Miyafusa
Shuichiro
S
Goda
Keisuke
K
Ishii
Tadashi
T
Matsuura
Yukio
Y
Sudou
Tatsuhiko
T
Kodama
Takao
T
Hamakubo
Kouhei
K
Tsumoto
D015820:Cadherins / Q000737:chemistry* / Q000378:metabolism*; D002118:Calcium / Q000737:chemistry* / Q000378:metabolism*; D019281:Dimerization; D006801:Humans; D008954:Models, Biological; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D013816:Thermodynamics
D015820:Cadherins; D002118:Calcium