نتایج جستجو برای: binding oligomerization domain

تعداد نتایج: 764826  

2014
Andrew D. Weems Courtney R. Johnson Juan Lucas Argueso Michael A. McMurray

Septin proteins bind GTP and heterooligomerize into filaments with conserved functions across a wide range of eukaryotes. Most septins hydrolyze GTP, altering the oligomerization interfaces; yet mutations designed to abolish nucleotide binding or hydrolysis by yeast septins perturb function only at high temperatures. Here, we apply an unbiased mutational approach to this problem. Mutations caus...

Journal: :Turkish Journal of Pediatrics 2021

Background Granulomatous autoinflammatory diseases are monogenic syndromes caused by mutations in the region encoding nucleotide-binding domain of oligomerization domain-containing 2 gene. Blau syndrome and early-onset sarcoidosis familial sporadic forms same disease very rare. Many organ systems may be involved; however, neurologic involvement is infrequent. We reported a case encephalitis 12-...

Journal: :Science 1997
S M Soisson B MacDougall-Shackleton R Schleif C Wolberger

The crystal structure of the arabinose-binding and dimerization domain of the Escherchia coli gene regulatory protein AraC was determined in the presence and absence of L-arabinose. The 1.5 angstrom structure of the arabinose-bound molecule shows that the protein adopts an unusual fold, binding sugar within a beta barrel and completely burying the arabinose with the amino-terminal arm of the pr...

Journal: :Medical research archives 2023

Pulmonary Hypertension is a progressive vascular disease resulting from the tapering of pulmonary arteries causing high arterial blood pressure and ultimately right ventricular failure. A defining characteristic excessive remodeling that includes increased proliferation, fibrosis inflammation. There no outward cure for nor are there interventions effectively impede or reverse remodeling, resear...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2014
Diana M Mitrea Christy R Grace Marija Buljan Mi-Kyung Yun Nicholas J Pytel John Satumba Amanda Nourse Cheon-Gil Park M Madan Babu Stephen W White Richard W Kriwacki

Nucleophosmin (NPM1) is a multifunctional phospho-protein with critical roles in ribosome biogenesis, tumor suppression, and nucleolar stress response. Here we show that the N-terminal oligomerization domain of NPM1 (Npm-N) exhibits structural polymorphism by populating conformational states ranging from a highly ordered, folded pentamer to a highly disordered monomer. The monomer-pentamer equi...

Journal: :Journal of Molecular Recognition 2017

Journal: :The EMBO journal 2005
Stefano Stella Roberto Spurio Maurizio Falconi Cynthia L Pon Claudio O Gualerzi

Two types of two-hybrid systems demonstrate that the transcriptional repressor, nucleoid-associated protein H-NS (histone-like, nucleoid structuring protein) forms dimers and tetramers in vivo, the latter being the active form of the protein. The H-NS 'protein oligomerization' domain (N-domain) is unable to oligomerize in the absence of the intradomain linker while the 'DNA-binding' C-domain cl...

2007
Sarah L. Noton Elizabeth Medcalf Dawn Fisher Anne E. Mullin Debra Elton Paul Digard

The matrix (M1) protein of influenza A virus is a multifunctional protein that plays essential structural and functional roles in the virus life cycle. It drives virus budding and is the major protein component of the virion, where it forms an intermediate layer between the viral envelope and integral membrane proteins and the genomic ribonucleoproteins (RNPs). It also helps to control the intr...

2017
Melinda S Hanes Kelley W Moremen Richard D Cummings

Cosmc is an endoplasmic reticulum chaperone necessary for normal protein O-GalNAc glycosylation through regulation of T-synthase, its single client. Loss-of-function of Cosmc results in expression of the Tn antigen, which is associated with multiple human diseases including cancer. Despite intense interest in dysregulated expression of the Tn antigen, little is known about the structure and fun...

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