Conformational preference of 'CαNN' short peptide motif towards recognition of anions.

Among several 'anion binding motifs', the recently described 'C(α)NN' motif occurring in the loop regions preceding a helix, is conserved through evolution both in sequence and its conformation. To establish the significance of the conserved sequence and their intrinsic affinity...

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Autores principales:	Tridip Sheet, Subhrangshu Supakar, Raja Banerjee
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/0f96cdb27e574afa903be9c019da9363
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spelling	oai:doaj.org-article:0f96cdb27e574afa903be9c019da93632021-11-18T07:53:44ZConformational preference of 'CαNN' short peptide motif towards recognition of anions.1932-620310.1371/journal.pone.0057366https://doaj.org/article/0f96cdb27e574afa903be9c019da93632013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23516403/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Among several 'anion binding motifs', the recently described 'C(α)NN' motif occurring in the loop regions preceding a helix, is conserved through evolution both in sequence and its conformation. To establish the significance of the conserved sequence and their intrinsic affinity for anions, a series of peptides containing the naturally occurring 'C(α)NN' motif at the N-terminus of a designed helix, have been modeled and studied in a context free system using computational techniques. Appearance of a single interacting site with negative binding free-energy for both the sulfate and phosphate ions, as evidenced in docking experiments, establishes that the 'C(α)NN' segment has an intrinsic affinity for anions. Molecular Dynamics (MD) simulation studies reveal that interaction with anion triggers a conformational switch from non-helical to helical state at the 'C(α)NN' segment, which extends the length of the anchoring-helix by one turn at the N-terminus. Computational experiments substantiate the significance of sequence/structural context and justify the conserved nature of the 'C(α)NN' sequence for anion recognition through "local" interaction.Tridip SheetSubhrangshu SupakarRaja BanerjeePublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 3, p e57366 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Tridip Sheet Subhrangshu Supakar Raja Banerjee Conformational preference of 'CαNN' short peptide motif towards recognition of anions.
description	Among several 'anion binding motifs', the recently described 'C(α)NN' motif occurring in the loop regions preceding a helix, is conserved through evolution both in sequence and its conformation. To establish the significance of the conserved sequence and their intrinsic affinity for anions, a series of peptides containing the naturally occurring 'C(α)NN' motif at the N-terminus of a designed helix, have been modeled and studied in a context free system using computational techniques. Appearance of a single interacting site with negative binding free-energy for both the sulfate and phosphate ions, as evidenced in docking experiments, establishes that the 'C(α)NN' segment has an intrinsic affinity for anions. Molecular Dynamics (MD) simulation studies reveal that interaction with anion triggers a conformational switch from non-helical to helical state at the 'C(α)NN' segment, which extends the length of the anchoring-helix by one turn at the N-terminus. Computational experiments substantiate the significance of sequence/structural context and justify the conserved nature of the 'C(α)NN' sequence for anion recognition through "local" interaction.
format	article
author	Tridip Sheet Subhrangshu Supakar Raja Banerjee
author_facet	Tridip Sheet Subhrangshu Supakar Raja Banerjee
author_sort	Tridip Sheet
title	Conformational preference of 'CαNN' short peptide motif towards recognition of anions.
title_short	Conformational preference of 'CαNN' short peptide motif towards recognition of anions.
title_full	Conformational preference of 'CαNN' short peptide motif towards recognition of anions.
title_fullStr	Conformational preference of 'CαNN' short peptide motif towards recognition of anions.
title_full_unstemmed	Conformational preference of 'CαNN' short peptide motif towards recognition of anions.
title_sort	conformational preference of 'cαnn' short peptide motif towards recognition of anions.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/0f96cdb27e574afa903be9c019da9363
work_keys_str_mv	AT tridipsheet conformationalpreferenceofcannshortpeptidemotiftowardsrecognitionofanions AT subhrangshusupakar conformationalpreferenceofcannshortpeptidemotiftowardsrecognitionofanions AT rajabanerjee conformationalpreferenceofcannshortpeptidemotiftowardsrecognitionofanions
_version_	1718422772121600000

Conformational preference of 'CαNN' short peptide motif towards recognition of anions.

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