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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ftsmithonian:oai:figshare.com:article/17130536 2023-05-15T14:17:07+02:00 Sequence alignments of individual EC repeats of CDHR5. Michelle E. Gray (7339328) Zachary R. Johnson (11797913) Debadrita Modak (11797916) Elakkiya Tamilselvan (11797919) Matthew J. Tyska (11797922) Marcos Sotomayor (1287807) 2021-12-06T18:27:12Z https://doi.org/10.1371/journal.pbio.3001463.s002 unknown https://figshare.com/articles/journal_contribution/Sequence_alignments_of_individual_EC_repeats_of_CDHR5_/17130536 doi:10.1371/journal.pbio.3001463.s002 CC BY 4.0 CC-BY 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 Text Journal contribution 2021 ftsmithonian https://doi.org/10.1371/journal.pbio.3001463.s002 2021-12-19T20:06:06Z 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) Other Non-Article Part of Journal/Newspaper Aptenodytes forsteri Unknown Parus ENVELOPE(3.950,3.950,-71.983,-71.983) |
institution |
Open Polar |
collection |
Unknown |
op_collection_id |
ftsmithonian |
language |
unknown |
topic |
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 |
spellingShingle |
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 Michelle E. Gray (7339328) Zachary R. Johnson (11797913) Debadrita Modak (11797916) Elakkiya Tamilselvan (11797919) Matthew J. Tyska (11797922) Marcos Sotomayor (1287807) Sequence alignments of individual EC repeats of CDHR5. |
topic_facet |
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 |
description |
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) |
format |
Other Non-Article Part of Journal/Newspaper |
author |
Michelle E. Gray (7339328) Zachary R. Johnson (11797913) Debadrita Modak (11797916) Elakkiya Tamilselvan (11797919) Matthew J. Tyska (11797922) Marcos Sotomayor (1287807) |
author_facet |
Michelle E. Gray (7339328) Zachary R. Johnson (11797913) Debadrita Modak (11797916) Elakkiya Tamilselvan (11797919) Matthew J. Tyska (11797922) Marcos Sotomayor (1287807) |
author_sort |
Michelle E. Gray (7339328) |
title |
Sequence alignments of individual EC repeats of CDHR5. |
title_short |
Sequence alignments of individual EC repeats of CDHR5. |
title_full |
Sequence alignments of individual EC repeats of CDHR5. |
title_fullStr |
Sequence alignments of individual EC repeats of CDHR5. |
title_full_unstemmed |
Sequence alignments of individual EC repeats of CDHR5. |
title_sort |
sequence alignments of individual ec repeats of cdhr5. |
publishDate |
2021 |
url |
https://doi.org/10.1371/journal.pbio.3001463.s002 |
long_lat |
ENVELOPE(3.950,3.950,-71.983,-71.983) |
geographic |
Parus |
geographic_facet |
Parus |
genre |
Aptenodytes forsteri |
genre_facet |
Aptenodytes forsteri |
op_relation |
https://figshare.com/articles/journal_contribution/Sequence_alignments_of_individual_EC_repeats_of_CDHR5_/17130536 doi:10.1371/journal.pbio.3001463.s002 |
op_rights |
CC BY 4.0 |
op_rightsnorm |
CC-BY |
op_doi |
https://doi.org/10.1371/journal.pbio.3001463.s002 |
_version_ |
1766289050778468352 |