NMR derived model of GTPase effector domain (GED) self association: relevance to dynamin assembly.

Self-association of dynamin to form spiral structures around lipidic vesicles during endocytosis is largely mediated by its 'coiled coil' GTPase Effector Domain (GED), which, in vitro, self-associates into huge helical assemblies. Residue-level structural characterizations of these assembl...

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Autores principales:	Swagata Chakraborty, Supriya Pratihar, Ramakrishna V Hosur
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/0d5b660758b64e9aa0e8b62ab4e5efd5
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spelling	oai:doaj.org-article:0d5b660758b64e9aa0e8b62ab4e5efd52021-11-18T07:30:20ZNMR derived model of GTPase effector domain (GED) self association: relevance to dynamin assembly.1932-620310.1371/journal.pone.0030109https://doaj.org/article/0d5b660758b64e9aa0e8b62ab4e5efd52012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22253896/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Self-association of dynamin to form spiral structures around lipidic vesicles during endocytosis is largely mediated by its 'coiled coil' GTPase Effector Domain (GED), which, in vitro, self-associates into huge helical assemblies. Residue-level structural characterizations of these assemblies and understanding the process of association have remained a challenge. It is also impossible to get folded monomers in the solution phase. In this context, we have developed here a strategy to probe the self-association of GED by first dissociating the assembly using Dimethyl Sulfoxide (DMSO) and then systematically monitoring the refolding into helix and concomitant re-association using NMR spectroscopy, as DMSO concentration is progressively reduced. The short segment, Arg109 - Met116, acts as the nucleation site for helix formation and self-association. Hydrophobic and complementary charge interactions on the surfaces drive self-association, as the helices elongate in both the directions resulting in an antiparallel stack. A small N-terminal segment remains floppy in the assembly. Following these and other published results on inter-domain interactions, we have proposed a plausible mode of dynamin self assembly.Swagata ChakrabortySupriya PratiharRamakrishna V HosurPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 1, p e30109 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Swagata Chakraborty Supriya Pratihar Ramakrishna V Hosur NMR derived model of GTPase effector domain (GED) self association: relevance to dynamin assembly.
description	Self-association of dynamin to form spiral structures around lipidic vesicles during endocytosis is largely mediated by its 'coiled coil' GTPase Effector Domain (GED), which, in vitro, self-associates into huge helical assemblies. Residue-level structural characterizations of these assemblies and understanding the process of association have remained a challenge. It is also impossible to get folded monomers in the solution phase. In this context, we have developed here a strategy to probe the self-association of GED by first dissociating the assembly using Dimethyl Sulfoxide (DMSO) and then systematically monitoring the refolding into helix and concomitant re-association using NMR spectroscopy, as DMSO concentration is progressively reduced. The short segment, Arg109 - Met116, acts as the nucleation site for helix formation and self-association. Hydrophobic and complementary charge interactions on the surfaces drive self-association, as the helices elongate in both the directions resulting in an antiparallel stack. A small N-terminal segment remains floppy in the assembly. Following these and other published results on inter-domain interactions, we have proposed a plausible mode of dynamin self assembly.
format	article
author	Swagata Chakraborty Supriya Pratihar Ramakrishna V Hosur
author_facet	Swagata Chakraborty Supriya Pratihar Ramakrishna V Hosur
author_sort	Swagata Chakraborty
title	NMR derived model of GTPase effector domain (GED) self association: relevance to dynamin assembly.
title_short	NMR derived model of GTPase effector domain (GED) self association: relevance to dynamin assembly.
title_full	NMR derived model of GTPase effector domain (GED) self association: relevance to dynamin assembly.
title_fullStr	NMR derived model of GTPase effector domain (GED) self association: relevance to dynamin assembly.
title_full_unstemmed	NMR derived model of GTPase effector domain (GED) self association: relevance to dynamin assembly.
title_sort	nmr derived model of gtpase effector domain (ged) self association: relevance to dynamin assembly.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/0d5b660758b64e9aa0e8b62ab4e5efd5
work_keys_str_mv	AT swagatachakraborty nmrderivedmodelofgtpaseeffectordomaingedselfassociationrelevancetodynaminassembly AT supriyapratihar nmrderivedmodelofgtpaseeffectordomaingedselfassociationrelevancetodynaminassembly AT ramakrishnavhosur nmrderivedmodelofgtpaseeffectordomaingedselfassociationrelevancetodynaminassembly
_version_	1718423330739978240

NMR derived model of GTPase effector domain (GED) self association: relevance to dynamin assembly.

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