Conformational plasticity and evolutionary analysis of the myotilin tandem Ig domains
Abstract Myotilin is a component of the sarcomere where it plays an important role in organisation and maintenance of Z-disk integrity. This involves direct binding to F-actin and filamin C, a function mediated by its Ig domain pair. While the structures of these two individual domains are known, in...
Enregistré dans:
Auteurs principaux: | Vid Puž, Miha Pavšič, Brigita Lenarčič, Kristina Djinović-Carugo |
---|---|
Format: | article |
Langue: | EN |
Publié: |
Nature Portfolio
2017
|
Sujets: | |
Accès en ligne: | https://doaj.org/article/c9ab95b6f7574c8ab9cb2d8daa190733 |
Tags: |
Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!
|
Documents similaires
-
Tandem domain structure determination based on a systematic enumeration of conformations
par: Thérèse E. Malliavin
Publié: (2021) -
Evolutionary plasticity of the NHL domain underlies distinct solutions to RNA recognition
par: Pooja Kumari, et autres
Publié: (2018) -
The Pseudomonas aeruginosa catabolite repression control protein Crc is devoid of RNA binding activity.
par: Tetyana Milojevic, et autres
Publié: (2013) -
Structural and biochemical studies on ATP binding and hydrolysis by the Escherichia coli RNA chaperone Hfq.
par: Hermann Hämmerle, et autres
Publié: (2012) -
Conformational analysis of isolated domains of Helicobacter pylori CagA.
par: Amanda P Woon, et autres
Publié: (2013)