Sequence alignments of individual EC repeats of CDHR5.

Multiple sequence alignments comparing each EC repeat of CDHR5 from 13 different species, shown as in S1 Fig . An asterisk (*) indicates site R84 mutated in binding assays. An arrow indicates the end of EC1-EC4 protein fragments used in binding assays. Secondary structure elements observed in the cr...

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Bibliographic Details
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
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Online Access:https://doi.org/10.1371/journal.pbio.3001463.s002
Description
Summary:Multiple sequence alignments comparing each EC repeat of CDHR5 from 13 different species, shown as in S1 Fig . An asterisk (*) indicates site R84 mutated in binding assays. An arrow indicates the end of EC1-EC4 protein fragments used in binding assays. Secondary structure elements observed in the crystal structures of hs CDHR5 EC1-2 are illustrated below the respective repeats. 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 and taxonomical diversity. Accession numbers and species can be found in S2 Table . CDHR5, cadherin-related family member 5; EC, extracellular cadherin. (PDF)