dc.contributor.author
Jurk, Claudia M.
dc.contributor.author
Roske, Yvette
dc.contributor.author
Heinemann, Udo
dc.date.accessioned
2018-11-05T12:51:53Z
dc.date.available
2018-11-05T12:51:53Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/23173
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-965
dc.description.abstract
Among the major components of the Golgi apparatus are the GRASP family proteins, including GRASP65 on the cis-Golgi side. With its GRASP domain, GRASP65 is involved in Golgi stacking and ribbon formation. Interaction of GRASP65 with the Golgi marker protein GM130 is important for the docking of vesicles to the Golgi membrane. We present here structures of the two individual PDZ domains comprising the GRASP domain in human GRASP65. We use isothermal titration calorimetry to probe the interaction between GRASP65 and GM130. Additionally, we present evidence for the limited sequence conservation of the PDZ fold by describing the PDZ domain structure of the GRASP65 homolog Grh1 from Saccharomyces cerevisiae.
en
dc.rights.uri
https://creativecommons.org/licenses/by/4.0/
dc.subject
PDZ domain structure
en
dc.subject
Golgi stacking
en
dc.subject
GRASP family
en
dc.subject
Golgi apparatus
en
dc.subject
yeast homolog of GRASP65
en
dc.subject
vesicle transport
en
dc.subject.ddc
500 Naturwissenschaften und Mathematik::540 Chemie::540 Chemie und zugeordnete Wissenschaften
dc.title
Crystal Structures of the Single PDZ Domains from GRASP65 and their Interaction with the Golgin GM130
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation.doi
10.5562/cca3341
dcterms.bibliographicCitation.journaltitle
Croat. Chem. Acta
dcterms.bibliographicCitation.number
2
dcterms.bibliographicCitation.pagestart
255
dcterms.bibliographicCitation.pageend
264
dcterms.bibliographicCitation.volume
91
dcterms.bibliographicCitation.url
http://pubweb.carnet.hr/ccacaa/
refubium.affiliation
Biologie, Chemie, Pharmazie
refubium.note.author
Der Artikel wurde in einer reinen Open-Access-Zeitschrift publiziert.
refubium.resourceType.isindependentpub
no
dcterms.accessRights.openaire
open access
dcterms.isPartOf.issn
0011-1643 (Print)
dcterms.isPartOf.issn
1334-417X (Online)