Title : Structural and biochemical studies of the extracellular domain of
Myelin protein zero-like protein 1
Abstract :
- Myelin protein zero-like protein 1 ( MPZL1 ) is a member of the immunoglobulin superfamily, and is also a receptor of concanavalin A (ConA)
- MPZL1 is upregulated in hepatocellular carcinoma (HCC) and accelerates migration of HCC cells
- However, function of MPZL1 as a receptor of ConA and its role in HCC development are largely unknown
- To elucidate the functional basis, we have determined the crystal structure of the extracellular domain of MPZL1 at 2.7 Å resolution
- Overall, it folds like a typical immunoglobulin variable-like domain that is much like MPZ
- Unexpectedly, we found Asn50 is a unique glycosylation site and the glycosylation mediates its interaction with ConA
- Furthermore, we also found that MPZL1 exists as a homodimer in the crystal, in which hydrogen bonds between Ser86 and Val145 play an important role
- Our results demonstrate that glycosylation of Asn50 is essential for its function as a receptor of ConA
- We propose that dimerization of MPZL1 participates in control of its signal transmission in cell adhesion