نتایج جستجو برای: glycine rich loop

تعداد نتایج: 311334  

Journal: :Journal of cell science 1996
J C Zabala A Fontalba J Avila

Tubulins contain a glycine-rich loop, that has been implicated in microtubule dynamics by means of an intramolecular interaction with the carboxy-terminal region. As a further extension of the analysis of the role of the carboxy-terminal region in tubulin folding we have mutated the glycine-rich loop of tubulin subunits. An alpha-tubulin point mutant with a T150-->G substitution (the correspond...

Journal: :Biochemical and biophysical research communications 2009
Hyo Sang Jang Jeffrey A Greenwood

Cysteine-rich protein 1 (CRP1) has a unique structure with two well separated LIM domains, each followed by a glycine-rich region. Although CRP1 has been shown to interact with actin-binding proteins and actin filaments, the mechanism regulating localization to the actin cytoskeleton in cells is not clear. Experiments using truncated forms showed that the first LIM domain and glycine-rich regio...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1999
Y Kai H Matsumura T Inoue K Terada Y Nagara T Yoshinaga A Kihara K Tsumura K Izui

The crystal structure of phosphoenolpyruvate carboxylase (PEPC; EC 4. 1.1.31) has been determined by x-ray diffraction methods at 2.8-A resolution by using Escherichia coli PEPC complexed with L-aspartate, an allosteric inhibitor of all known PEPCs. The four subunits are arranged in a "dimer-of-dimers" form with respect to subunit contact, resulting in an overall square arrangement. The content...

2011
Boris Rogelj Katherine S. Godin Christopher E. Shaw Jernej Ule

Glycine‐rich regions form intrinsically unstructured domains within RNA‐binding proteins. Although they lack a defined structure when alone in solution, these domains can form more defined structural elements when interacting with other proteins or with RNA. TDP‐43 and FUS are RNA binding proteins with glycine‐rich domains that form abnormal aggregates in amyotrophic lateral sclerosis (ALS) and...

2014
Iván Plaza-Menacho Karin Barnouin Kerry Goodman Rubén J. Martínez-Torres Annabel Borg Judith Murray-Rust Stephane Mouilleron Phillip Knowles Neil Q. McDonald

To decipher the molecular basis for RET kinase activation and oncogenic deregulation, we defined the temporal sequence of RET autophosphorylation by label-free quantitative mass spectrometry. Early autophosphorylation sites map to regions flanking the kinase domain core, while sites within the activation loop only form at later time points. Comparison with oncogenic RET kinase revealed that lat...

Journal: :Molecular cell 2009
Rina Barouch-Bentov Jianwei Che Christian C Lee Yating Yang Ann Herman Yong Jia Anastasia Velentza James Watson Luise Sternberg Sunjun Kim Niusha Ziaee Andrew Miller Carie Jackson Manabu Fujimoto Mike Young Serge Batalov Yi Liu Markus Warmuth Tim Wiltshire Michael P Cooke Karsten Sauer

The glycine-rich G loop controls ATP binding and phosphate transfer in protein kinases. Here we show that the functions of Src family and Abl protein tyrosine kinases require an electrostatic interaction between oppositely charged amino acids within their G loops that is conserved in multiple other phylogenetically distinct protein kinases, from plants to humans. By limiting G loop flexibility,...

Journal: :The Journal of biological chemistry 1997
W Hemmer M McGlone I Tsigelny S S Taylor

A glycine-rich loop in the ATP-binding site is one of the most highly conserved sequence motifs in protein kinases. Each conserved glycine (Gly-50, Gly-52, and Gly-55) in the catalytic (C) subunit of cAMP-dependent protein kinase (cAPK) was replaced with Ser and/or Ala. Active mutant proteins were expressed in Escherichia coli, purified to apparent homogeneity, separated into phosphoisoforms, a...

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