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Influence of proline residues in transmembrane helix packing

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Influence of proline residues in transmembrane helix packing

dc.contributor.author	Orzáez Calatayud, María del Mar
dc.contributor.author	Salgado Benito, Jesús
dc.contributor.author	Giménez-Giner, Ana
dc.contributor.author	Pérez Payá, Enrique
dc.contributor.author	Mingarro Muñoz, Ismael
dc.date.accessioned	2018-04-17T13:34:46Z
dc.date.available	2018-04-17T13:34:46Z
dc.date.issued	2004
dc.identifier.citation	Orzáez Calatayud, María del Mar Salgado Benito, Jesús Giménez-Giner, Ana Pérez Payá, Enrique Mingarro Muñoz, Ismael 2004 Influence of proline residues in transmembrane helix packing Journal of Molecular Biology 335 2 631 640
dc.identifier.uri	http://hdl.handle.net/10550/65751
dc.description.abstract	Integral membrane proteins often contain proline residues in their alpha-helical transmembrane (TM) fragments, which may strongly influence their folding and association. Pro-scanning mutagenesis of the helical domain of glycophorin A (GpA) showed that replacement of the residues located at the center abrogates helix packing while substitution of the residues forming the ending helical turns allows dimer formation. Synthetic TM peptides revealed that a point mutation of one of the residues of the dimerization motif (L75P) located at the N-terminal helical turn of the GpA TM fragment, adopts a secondary structure and oligomeric state similar to the wild-type sequence in detergents. In addition, both glycosylation mapping in biological membranes and molecular dynamics showed that the presence of a proline residue at the lipid/water interface has as an effect the extension of the helical end. Thus, helix packing can be an important factor that determines appearance of proline in TM helices. Membrane proteins might accumulate proline residues at the two ends of their TM segments in order to modulate the exposition of key amino acid residues at the interface for molecular recognition events while allowing stable association and native folding.
dc.language.iso	eng
dc.relation.ispartof	Journal of Molecular Biology, 2004, vol. 335, num. 2, p. 631-640
dc.subject	Proteïnes de membrana
dc.title	Influence of proline residues in transmembrane helix packing
dc.type	journal article	es_ES
dc.date.updated	2018-04-17T13:34:47Z
dc.identifier.doi	10.1016/j.jmb.2003.10.062
dc.identifier.idgrec	000683
dc.rights.accessRights	open access	es_ES