1. Αποθετήριο Παραδοτέων Υποτρόφων Δράσεων ΕΣΠΑ Τριτοβάθμιας Εκπαίδευσης 2017-2023
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Τύπος:	Άρθρο σε επιστημονικό περιοδικό
Τίτλος:	1H, 13C, 15N backbone and side-chain resonance assignment of the native form of UbcH7 (UBE2L3) through solution NMR spectroscopy
Συγγραφέας:	[EL] Μαρούσης, Κωνσταντίνος [EL] Μπίρκου, Μαρία[EN] Birkou, Maria [EL] Asimakopoulou, Antonia [EL] Σπυρούλιας, Γεώργιος[EN] Spyroulias, Georgios
Ημερομηνία:	02/12/2019
Περίληψη:	Ubiquitination is a post-translational modification that regulates a plethora of processes in cells. Ubiquitination requires three type of enzyme: E1 ubiquitin (Ub) activating enzymes, E2 Ub conjugating enzymes and E3 ubiquitin ligases. The E2 enzymes perform a variety of functions, as Ub chain initiation, elongation and regulation of the topology and the process of chain formation. The E2 enzymes family is mainly characterized by a highly conserved ubiquitin conjugating domain (UBC), which comprises the binding region for the activated Ub, E1 and E3 enzymes. The E2 enzyme UbcH7 (UBE2L3) is a known interacting partner for different types of E3 Ub ligases such as HECT, RING and RBR. A structural analysis of the apo form of the native UbcH7 will provide the structural information to understand how this E2 enzyme is implicated in a wide range of diseases and how it interacts with its partners. In the present study we present the high yield expression of the native UbcH7 E2 enzyme and its preliminary analysis via solution NMR spectroscopy. The E2 enzyme is folded in solution and nearly a complete backbone assignment was achieved. Additionally, TALOS+ analysis was performed and the results indicated that UbcH7 adopts a αββββααα topology which is similar to that of the majority of E2 enzymes.
Γλώσσα:	Αγγλικά
Σελίδες:	6
DOI:	10.1007/s12104-019-09923-9
ISSN:	1874-2718
Θεματική κατηγορία:	[EL] Επιστήμες Υγείας[EN] Health Sciences
Λέξεις-κλειδιά:	UbcH7; E2 enzyme; UBC; · Solution NMR spectroscopy; Secondary structure; UBE2L3
Κάτοχος πνευματικών δικαιωμάτων:	© Springer Nature B.V. 2019
Ηλεκτρονική διεύθυνση του τεκμηρίου στον εκδότη:	https://link.springer.com/article/10.1007/s12104-019-09923-9
Ηλεκτρονική διεύθυνση περιοδικού:	https://www.springer.com/journal/12104
Τίτλος πηγής δημοσίευσης:	Biomolecular NMR Assignments
Τεύχος:	1
Τόμος:	14
Σελίδες τεκμηρίου (στην πηγή):	73-78
Σημειώσεις:	NSRF 2014–2020 "Support researchers with emphasis on young researchers” Grant (MIS 5005906/80499) is acknowledged for financial support of this work. Anastasia Seliami is acknowledged for her contribution in this work.
Εμφανίζεται στις συλλογές:	Ερευνητικές ομάδες