Rational design of a novel calcium-binding site adjacent to the ligand-binding site on CD2 increases its CD48 affinity.

ABSTRACT: Electrostatic interactions are important for molecular recognition processes including Ca2+-binding and cell adhesion. To understand these processes, we have successfully introduced a novel Ca2+-binding site into the non-Ca2+-dependent cell adhesion protein CD2 using our criteria that are specifically tailored to the structural and functional properties of the protein environment and charged adhesion surface. This designed site with ligand residues exclusively from the beta-sheets selectively binds to Ca2+ and Ln3+ over other mono- and divalent cations. While Ca2+ and Ln3+ binding specifically alters the local environment of the designed Ca2+-binding site, the designed protein undergoes a significantly smaller conformation change compared with those observed in naturally occurring Ca2+-bin

SUBMITTER: Jones LM 

PROVIDER: S-EPMC2248323 | biostudies-literature | 2008 Mar

REPOSITORIES: biostudies-literature