Sequence alignments of individual EC repeats of PCDH24.

• Main Authors: Michelle E. Gray (7339328), Zachary R. Johnson (11797913), Debadrita Modak (11797916), Elakkiya Tamilselvan (11797919), Matthew J. Tyska (11797922), Marcos Sotomayor (1287807)
• Format: Other Non-Article Part of Journal/Newspaper
• Language: unknown
• Published: 2021
• Subjects: Biophysics; Biochemistry; Cell Biology; Physiology; Biotechnology; Developmental Biology; Marine Biology; Cancer; Infectious Diseases; Chemical Sciences not elsewhere classified; Physical Sciences not elsewhere classified; xlink "> enterocytes; use binding assays; specific features relevant; ray crystal structures; hexagonal pattern maintained; 2 nonclassical members; interactions remain unresolved; intestinal intermicrovillar links; intermicrovillar links formed; homophilic interactions important; cdhr5 extracellular tips; homophilic cadherin interactions; cdhr5 domains involved; extracellular domains; adhesive interactions; intermicrovillar function; cadherin superfamily; homophilic adhesion; cdhr5 ); structural determinants; small intestine; results suggest; present x; microvilli known; luminal surface; brush borders; also known; Parus; Aptenodytes forsteri
• Online Access: https://doi.org/10.1371/journal.pbio.3001463.s001

Multiple sequence alignments comparing each EC repeat and MAD10 of PCDH24 from 13 different species. Each alignment is colored by percent identity, with white being the lowest percent identity and dark blue being the highest. Sites of N-linked (blue in human, green in mouse) and O-linked (purple in human, red in mouse) glycosylation are denoted by a colored circle. An asterisk (*) indicates sites Y67 and Y71 mutated in binding assays. Secondary structure elements observed in the crystal structures of hs PCDH24 EC1-2 and mm PCDH24 EC1-3 are illustrated below the respective repeats. Residues at the antiparallel homophilic hs PCDH24 EC1-2 II interface (>30% buried surface area) are denoted by a light blue bar. Calcium-binding motifs are indicated above the sequences, which are numbered according to the human protein. Species are abbreviated as follows: Homo sapiens ( Hs ), Mus musculus ( Mm ), Sus scrofa ( Ss ), Gallus gallus ( Gg ), Aptenodytes forsteri ( Af ), Parus major ( Pm ), Anolis carolinensis ( Ac ), Crocodylus porosus ( Cp ), Thamnophis elegans ( Te ), Danio rerio ( Dr ), Oryzias melastigma ( Om ), Mastacembelus armatus ( Ma ), and Xenopus tropicalis ( Xt ). Species were chosen based on sequence availability, coverage of entire extracellular domain, and taxonomical diversity. Accession numbers and species can be found in S2 Table . EC, extracellular cadherin; PCDH24, protocadherin-24. (PDF)