Resonance assignment of the Shank1 PDZ domain

Shank proteins are among the most abundant and well-studied postsynaptic scaffold proteins. Their PDZ domain has unique characteristics as one of its loop regions flanking the ligand-binding site is uniquely long and has also been implicated in the formation of PDZ dimers. Here we report the initial...

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Bibliographic Details
Main Authors: Sánta Anna
Czajlik András
Batta Gyula
Péterfia Bálint
Gáspári Zoltán
Format: Article
Published: 2022
Series:BIOMOLECULAR NMR ASSIGNMENTS 16 No. 1
Subjects:
mtmt:32625251
Online Access:https://publikacio.ppke.hu/1621

MARC

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520 3 |a Shank proteins are among the most abundant and well-studied postsynaptic scaffold proteins. Their PDZ domain has unique characteristics as one of its loop regions flanking the ligand-binding site is uniquely long and has also been implicated in the formation of PDZ dimers. Here we report the initial characterization of the Shank1 PDZ domain by solution NMR spectroscopy. The assigned chemical shifts are largely consistent with the common features of PDZ domains in general and the available Shank PDZ crystal structures in particular. Our analysis suggests that under the conditions investigated, the domain is monomeric and the unique loop harbors a short helical segment, observed in only one of the known X-ray structures so far. Our work stresses the importance of solution-state investigations to fully decipher the functional relevance of the structural and dynamical features unique to Shank PDZ domains. 
650 4 |a Biokémia és molekuláris biológia 
700 0 1 |a Czajlik András  |e aut 
700 0 1 |a Batta Gyula  |e aut 
700 0 1 |a Péterfia Bálint  |e aut 
700 0 1 |a Gáspári Zoltán  |e aut 
856 4 0 |u https://publikacio.ppke.hu/id/eprint/1621/1/biomolecularnmr21.10.11.pdf  |z Dokumentum-elérés