منابع مشابه
Calponin-Like Chd64 Is Partly Disordered
20-hydroxyecdysone (20E) and juvenile hormone (JH) signaling pathways interact to regulate insect development. Recently, two proteins, a calponin-like Chd64 and immunophilin FKBP39 have been found to play a pivotal role in the cross-talk between 20E and JH, although the molecular basis of interaction remains unknown. The aim of this work was to identify the structural features that would provid...
متن کاملInsight into the Unfolding Properties of Chd64, a Small, Single Domain Protein with a Globular Core and Disordered Tails
Two major lipophilic hormones, 20-hydroxyecdysone (20E) and juvenile hormone (JH), govern insect development and growth. While the mode of action of 20E is well understood, some understanding of JH-dependent signalling has been attained only in the past few years, and the crosstalk of the two hormonal pathways remains unknown. Two proteins, the calponin-like Chd64 and immunophilin FKBP39 protei...
متن کاملNucleoplasmin-like domain of FKBP39 from Drosophila melanogaster forms a tetramer with partly disordered tentacle-like C-terminal segments
Nucleoplasmins are a nuclear chaperone family defined by the presence of a highly conserved N-terminal core domain. X-ray crystallographic studies of isolated nucleoplasmin core domains revealed a β-propeller structure consisting of a set of five monomers that together form a stable pentamer. Recent studies on isolated N-terminal domains from Drosophila 39-kDa FK506-binding protein (FKBP39) and...
متن کاملVascular smooth muscle calponin. A novel troponin T-like protein.
In a search for additional Ca2+ regulatory components in vascular smooth muscle, a novel troponin T-like protein was purified from bovine aorta smooth muscle. The isolated protein was separated into several isoforms on isoelectric focusing. The major isoelectric variants were focused in the pH region of 8.4 to 9.1. The protein had slightly different molecular masses in the Mr range of 35,000 on...
متن کاملDystrophin's tandem calponin-homology domains: is the case closed?
Actin plays a central role in the eukaryotic cytoskeleton and interacts with a large number of proteins (1). The actin-binding domains in these proteins have been classified into different groups based on structural similarity. A repeat of two calponin-homology domains (designated CH1-CH2) constitutes one major class of low-affinity actin-binding domains (ABDs) (2,3). Despite the abundance and ...
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ژورنال
عنوان ژورنال: PLoS ONE
سال: 2014
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0096809