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Intrapolypeptide Interactions between the GTPase Effector Domain (GED) and the GTPase Domain Form the Bundle Signaling Element in Dynamin Dimers

[Image: see text] Biochemical and structural studies of dynamin have shown that the C-terminus of the GTPase effector domain (GED) folds back and docks onto a platform created by the N- and C-terminal α-helices of the GTPase domain to form a three-helix bundle. While cross-linking studies suggested...

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Autores principales: Srinivasan, Saipraveen, Mattila, Juha-Pekka, Schmid, Sandra L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2014
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4166026/
https://www.ncbi.nlm.nih.gov/pubmed/25171143
http://dx.doi.org/10.1021/bi500998s
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author Srinivasan, Saipraveen
Mattila, Juha-Pekka
Schmid, Sandra L.
author_facet Srinivasan, Saipraveen
Mattila, Juha-Pekka
Schmid, Sandra L.
author_sort Srinivasan, Saipraveen
collection PubMed
description [Image: see text] Biochemical and structural studies of dynamin have shown that the C-terminus of the GTPase effector domain (GED) folds back and docks onto a platform created by the N- and C-terminal α-helices of the GTPase domain to form a three-helix bundle. While cross-linking studies suggested that insect cell-expressed dynamin existed as a domain-swapped dimer, X-ray structures of protein expressed in Escherichia coli failed to detect evidence of this domain swap. Here, by cross-linking several cysteine pair replacements and analyzing cross-linked species by matrix-assisted laser desorption ionization Mega time of flight, we conclude that dynamin is not domain-swapped and that GED–GTPase domain interactions occur in cis.
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spelling pubmed-41660262015-08-29 Intrapolypeptide Interactions between the GTPase Effector Domain (GED) and the GTPase Domain Form the Bundle Signaling Element in Dynamin Dimers Srinivasan, Saipraveen Mattila, Juha-Pekka Schmid, Sandra L. Biochemistry [Image: see text] Biochemical and structural studies of dynamin have shown that the C-terminus of the GTPase effector domain (GED) folds back and docks onto a platform created by the N- and C-terminal α-helices of the GTPase domain to form a three-helix bundle. While cross-linking studies suggested that insect cell-expressed dynamin existed as a domain-swapped dimer, X-ray structures of protein expressed in Escherichia coli failed to detect evidence of this domain swap. Here, by cross-linking several cysteine pair replacements and analyzing cross-linked species by matrix-assisted laser desorption ionization Mega time of flight, we conclude that dynamin is not domain-swapped and that GED–GTPase domain interactions occur in cis. American Chemical Society 2014-08-29 2014-09-16 /pmc/articles/PMC4166026/ /pubmed/25171143 http://dx.doi.org/10.1021/bi500998s Text en Copyright © 2014 American Chemical Society Terms of Use (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html)
spellingShingle Srinivasan, Saipraveen
Mattila, Juha-Pekka
Schmid, Sandra L.
Intrapolypeptide Interactions between the GTPase Effector Domain (GED) and the GTPase Domain Form the Bundle Signaling Element in Dynamin Dimers
title Intrapolypeptide Interactions between the GTPase Effector Domain (GED) and the GTPase Domain Form the Bundle Signaling Element in Dynamin Dimers
title_full Intrapolypeptide Interactions between the GTPase Effector Domain (GED) and the GTPase Domain Form the Bundle Signaling Element in Dynamin Dimers
title_fullStr Intrapolypeptide Interactions between the GTPase Effector Domain (GED) and the GTPase Domain Form the Bundle Signaling Element in Dynamin Dimers
title_full_unstemmed Intrapolypeptide Interactions between the GTPase Effector Domain (GED) and the GTPase Domain Form the Bundle Signaling Element in Dynamin Dimers
title_short Intrapolypeptide Interactions between the GTPase Effector Domain (GED) and the GTPase Domain Form the Bundle Signaling Element in Dynamin Dimers
title_sort intrapolypeptide interactions between the gtpase effector domain (ged) and the gtpase domain form the bundle signaling element in dynamin dimers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4166026/
https://www.ncbi.nlm.nih.gov/pubmed/25171143
http://dx.doi.org/10.1021/bi500998s
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