Human Calmodulin-Like Protein 5, CALML5 Primacu™ ELI

Calmodulin-like protein 5, also known as Calmodulin-like skin protein, CALML5 and CLSP, is a protein which contains fourEF-hand domains.

CALML5 / CLSP is particularly abundant in the epidermis where its expression is directly related to keratinocyte differentiation.The expression is very low in lung.

CALML5 / CLSP binds calcium.

It may be involved in terminal differentiation of keratinocytes.

Coxsackievirus and adenovirus receptor (CAR) is a member of the immunoglobulin (Ig) superfamily and a component of epithelial tight junction.

CAR functions as a primary receptor for coxsackievirus B and adenovirus (Ad) infection.

CALML5 / CLSP is closely related to CAR.

The structure and dynamics of human calmodulin-like skin protein CALML5 / CLSP have been characterized by NMR spectroscopy.

The mobility of CALML5 / CLSP has been found to be different for the N-terminal and C-terminal domains.

The N-terminal domain is characterized by four stable helices, which experience large fluctuations.

This is shown to be due to mutations in the hydrophobic core.

The overall N-terminal domain behavior is similar both in the full-length protein and in the isolated domain.