Issue 8, 2012

Structural and thermodynamic characterization of the self-adhesive properties of human P-cadherin

Abstract

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 proteinprotein complex.

Graphical abstract: Structural and thermodynamic characterization of the self-adhesive properties of human P-cadherin

Supplementary files

Article information

Article type
Communication
Submitted
26 Apr 2012
Accepted
22 May 2012
First published
24 May 2012

Mol. BioSyst., 2012,8, 2050-2053

Structural and thermodynamic characterization of the self-adhesive properties of human P-cadherin

S. Kudo, J. M. M. Caaveiro, T. Miyafusa, S. Goda, K. Ishii, T. Matsuura, Y. Sudou, T. Kodama, T. Hamakubo and K. Tsumoto, Mol. BioSyst., 2012, 8, 2050 DOI: 10.1039/C2MB25161B

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Spotlight

Advertisements