Nectin

For all nectins the intracellular domain can bind a scaffold protein named afadin (the product of the MLLT4 gene).[4] Recent structural reports reveal the physical and chemical determinants of homophilic interactions mediated by N-terminal IgV domains.Nectins and Necls are much related in function and protein structure and have been found to interact in a variety of way, which it is why it makes good sense to define them as families.Unlike many other cellular adhesion molecules they do not distribute evenly on axonal and dendritic side of the synapse.Nectin-4 : Enfortumab vedotin-ejfv was approved by the FDA in 2019; it is a Nectin-4-directed antibody drug conjugate that has shown clinical activity in metastatic urothelial cancer.
Membranomecellular adhesion moleculescellular adhesionadherens junctionepitheliachemical synapsenectin-1nectin-2nectin-3nectin-4Necl-1Necl-2Necl-5immunoglobulin domainsscaffold proteincadherinsEnfortumab vedotin-ejfvMedical Subject HeadingsMembrane proteinscell adhesion moleculesIgSF CAMMyelin protein zeroVCAM-1PE-CAML1 familyL1-CAMIntegrinsIntegrin alphaXbeta2Macrophage-1 antigenGlycoprotein IIb/IIIaITGA2BDesmosomalDesmogleinDesmocollinProtocadherinPCDH15PCDH19T-cadherinSelectinsE-selectinL-selectinP-selectinLymphocyte homing receptorintegrinCarcinoembryonic antigen