Gutenberg Open Science: Small residues inhibit homo-dimerization of the human carbonic anhydrase XII transmembrane domain

Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-6515

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DC Field	Value	Language
dc.contributor.author	Cymer, Florian	-
dc.contributor.author	Schneider, Dirk	-
dc.date.accessioned	2021-11-15T11:20:48Z	-
dc.date.available	2021-11-15T11:20:48Z	-
dc.date.issued	2021	-
dc.identifier.uri	https://openscience.ub.uni-mainz.de/handle/20.500.12030/6525	-
dc.description.abstract	Amino acids with small side chains and motifs of small residues in a distance of four are rather abundant in human single-span transmembrane helices. While interaction of such helices appears to be common, the role of the small residues in mediating and/or stabilizing transmembrane helix oligomers remains mostly elusive. Yet, the mere existence of (small)xxx(small) motifs in transmembrane helices is frequently used to model dimeric TM helix structures. The single transmembrane helix of the human carbonic anhydrases XII contains a large number of amino acids with small side chains, and critical involvement of these small amino acids in dimerization of the transmembrane domain has been suggested. Using the GALLEX assay, we show here that the transmembrane domain indeed forms a strong transmembrane helix oligomer within a biological membrane. However, single or multiple mutations of small residue(s) to isoleucine almost always increased, rather than decreased, the interaction propensities. Reduction of helix flexibility and of protein–lipid contacts caused by a reduced lipid accessible surface area likely results in stabilization of helix–helix interactions within the membrane.	en_GB
dc.description.sponsorship	Open Access-Publizieren Universität Mainz / Universitätsmedizin Mainz	de
dc.language.iso	eng	de
dc.rights	CC BY	*
dc.rights.uri	https://creativecommons.org/licenses/by/4.0/	*
dc.subject.ddc	540 Chemie	de_DE
dc.subject.ddc	540 Chemistry and allied sciences	en_GB
dc.subject.ddc	570 Biowissenschaften	de_DE
dc.subject.ddc	570 Life sciences	en_GB
dc.title	Small residues inhibit homo-dimerization of the human carbonic anhydrase XII transmembrane domain	en_GB
dc.type	Zeitschriftenaufsatz	de
dc.identifier.doi	http://doi.org/10.25358/openscience-6515	-
jgu.type.dinitype	article	en_GB
jgu.type.version	Published version	de
jgu.type.resource	Text	de
jgu.organisation.department	FB 09 Chemie, Pharmazie u. Geowissensch.	de
jgu.organisation.number	7950	-
jgu.organisation.name	Johannes Gutenberg-Universität Mainz	-
jgu.rights.accessrights	openAccess	-
jgu.journal.title	Membranes	de
jgu.journal.volume	11	de
jgu.journal.issue	7	de
jgu.pages.alternative	512	de
jgu.publisher.year	2021	-
jgu.publisher.name	MDPI	de
jgu.publisher.place	Basel	de
jgu.publisher.uri	https://doi.org/10.3390/membranes11070512	de
jgu.publisher.issn	2077-0375	de
jgu.organisation.place	Mainz	-
jgu.subject.ddccode	540	de
jgu.subject.ddccode	570	de
jgu.publisher.doi	10.3390/membranes11070512
jgu.organisation.ror	https://ror.org/023b0x485
Appears in collections:	JGU-Publikationen

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