scholarly journals Structural Basis for the Activation of Platelet Integrin αIIbβ3 by Calcium- and Integrin-Binding Protein 1

2012 ◽  
Vol 134 (8) ◽  
pp. 3864-3872 ◽  
Author(s):  
Hao Huang ◽  
Hans J. Vogel
Keyword(s):  
Binding Protein ◽  
Structural Basis ◽  
Integrin Αiibβ3

Structural Basis of the Broad Specificity of a General Odorant-Binding Protein from Honeybee

Biochemistry ◽  
2009 ◽  
Vol 48 (11) ◽  
pp. 2431-2441 ◽  
Author(s):  
Ewen Lescop ◽  
Loïc Briand ◽  
Jean-Claude Pernollet ◽  
Eric Guittet
Keyword(s):  
Binding Protein ◽  
Odorant Binding Protein ◽  
Structural Basis ◽  
Odorant Binding ◽  
Broad Specificity

Structural characterization of amorphous calcium carbonate-binding protein: an insight into the mechanism of amorphous calcium carbonate formation

2013 ◽  
Vol 453 (2) ◽  
pp. 179-186 ◽  
Author(s):  
Jingtan Su ◽  
Xiao Liang ◽  
Qiang Zhou ◽  
Guiyou Zhang ◽  
Hongzhong Wang ◽  
...  
Keyword(s):  
Calcium Carbonate ◽  
Binding Sites ◽  
Binding Protein ◽  
Homology Modelling ◽  
Size Exclusion ◽  
Structural Basis ◽  
Amorphous Calcium Carbonate ◽  
Carbonate Formation

ACC (amorphous calcium carbonate) plays an important role in biomineralization process for its function as a precursor for calcium carbonate biominerals. However, it is unclear how biomacromolecules regulate the formation of ACC precursor in vivo. In the present study, we used biochemical experiments coupled with bioinformatics approaches to explore the mechanisms of ACC formation controlled by ACCBP (ACC-binding protein). Size-exclusion chromatography, chemical cross-linking experiments and negative staining electron microscopy reveal that ACCBP is a decamer composed of two adjacent pentamers. Sequence analyses and fluorescence quenching results indicate that ACCBP contains two Ca2+-binding sites. The results of in vitro crystallization experiments suggest that one Ca2+-binding site is critical for ACC formation and the other site affects the ACC induction efficiency. Homology modelling demonstrates that the Ca2+-binding sites of pentameric ACCBP are arranged in a 5-fold symmetry, which is the structural basis for ACC formation. To the best of our knowledge, this is the first report on the structural basis for protein-induced ACC formation and it will significantly improve our understanding of the amorphous precursor pathway.

scholarly journals Structural basis of nucleic acid binding byNicotiana tabacumglycine-rich RNA-binding protein: implications for its RNA chaperone function

2014 ◽  
Vol 42 (13) ◽  
pp. 8705-8718 ◽  
Author(s):  
Fariha Khan ◽  
Mark A. Daniëls ◽  
Gert E. Folkers ◽  
Rolf Boelens ◽  
S. M. Saqlan Naqvi ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Structural Basis ◽  
Nucleic Acid Binding ◽  
Rna Chaperone ◽  
Chaperone Function

scholarly journals Structural basis of the zinc-induced cytoplasmic aggregation of the RNA-binding protein SFPQ

2020 ◽  
Vol 48 (6) ◽  
pp. 3356-3365 ◽  
Author(s):  
Jie Huang ◽  
Mitchell Ringuet ◽  
Andrew E Whitten ◽  
Sofia Caria ◽  
Yee Wa Lim ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Cortical Neurons ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Zinc Binding ◽  
Structural Basis ◽  
Rna Biogenesis ◽  
Cytoplasmic Accumulation ◽  
Nucleocytoplasmic Distribution

Abstract SFPQ is a ubiquitous nuclear RNA-binding protein implicated in many aspects of RNA biogenesis. Importantly, nuclear depletion and cytoplasmic accumulation of SFPQ has been linked to neuropathological conditions such as Alzheimer's disease (AD) and amyotrophic lateral sclerosis (ALS). Here, we describe a molecular mechanism by which SFPQ is mislocalized to the cytoplasm. We report an unexpected discovery of the infinite polymerization of SFPQ that is induced by zinc binding to the protein. The crystal structure of human SFPQ in complex with zinc at 1.94 Å resolution reveals intermolecular interactions between SFPQ molecules that are mediated by zinc. As anticipated from the crystal structure, the application of zinc to primary cortical neurons induced the cytoplasmic accumulation and aggregation of SFPQ. Mutagenesis of the three zinc-coordinating histidine residues resulted in a significant reduction in the zinc-binding affinity of SFPQ in solution and the zinc-induced cytoplasmic aggregation of SFPQ in cultured neurons. Taken together, we propose that dysregulation of zinc availability and/or localization in neuronal cells may represent a mechanism for the imbalance in the nucleocytoplasmic distribution of SFPQ, which is an emerging hallmark of neurodegenerative diseases including AD and ALS.

scholarly journals Structural Basis of Glycerophosphodiester Recognition by the Mycobacterium tuberculosis Substrate-Binding Protein UgpB

2019 ◽  
Vol 14 (9) ◽  
pp. 1879-1887 ◽  
Author(s):  
Jonathan S. Fenn ◽  
Ridvan Nepravishta ◽  
Collette S. Guy ◽  
James Harrison ◽  
Jesus Angulo ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Binding Protein ◽  
Substrate Binding ◽  
Structural Basis ◽  
Substrate Binding Protein

scholarly journals Structural Basis of Lipid Exchange in the Oxysterol-Binding Protein Homologue (OSH) Family

2014 ◽  
Vol 106 (2) ◽  
pp. 99a
Author(s):  
Stefano Vanni ◽  
Joachim Moser von Filseck ◽  
Bruno Mesmin ◽  
Bruno Antonny ◽  
Guillaume Drin
Keyword(s):  
Binding Protein ◽  
Structural Basis ◽  
Oxysterol Binding Protein ◽  
Lipid Exchange

scholarly journals Structural basis underlying CAC RNA recognition by the RRM domain of dimeric RNA-binding protein RBPMS

2015 ◽  
Vol 49 ◽  
Author(s):  
Marianna Teplova ◽  
Thalia A. Farazi ◽  
Thomas Tuschl ◽  
Dinshaw J. Patel
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Hek293 Cells ◽  
Structural Basis ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Binding Studies ◽  
Muscle Plasticity ◽  
Rrm Domain

AbstractRNA-binding protein with multiple splicing (designated RBPMS) is a higher vertebrate mRNA-binding protein containing a single RNA recognition motif (RRM). RBPMS has been shown to be involved in mRNA transport, localization and stability, with key roles in axon guidance, smooth muscle plasticity, as well as regulation of cancer cell proliferation and migration. We report on structure-function studies of the RRM domain of RBPMS bound to a CAC-containing single-stranded RNA. These results provide insights into potential topologies of complexes formed by the RBPMS RRM domain and the tandem CAC repeat binding sites as detected by photoactivatable-ribonucleoside-enhanced crosslinking and immunoprecipitation. These studies establish that the RRM domain of RBPMS forms a symmetrical dimer in the free state, with each monomer binding sequence-specifically to all three nucleotides of a CAC segment in the RNA bound state. Structure-guided mutations within the dimerization and RNA-binding interfaces of RBPMS RRM on RNA complex formation resulted in both disruption of dimerization and a decrease in RNA-binding affinity as observed by size exclusion chromatography and isothermal titration calorimetry. As anticipated from biochemical binding studies, over-expression of dimerization or RNA-binding mutants of Flag-HA-tagged RBPMS were no longer able to track with stress granules in HEK293 cells, thereby documenting the deleterious effects of such mutations in vivo.

scholarly journals Structural basis for cooperativity of human monoclonal antibodies to meningococcal factor H-binding protein

2019 ◽  
Vol 2 (1) ◽  
Author(s):  
Ilaria Peschiera ◽  
Maria Giuliani ◽  
Fabiola Giusti ◽  
Roberto Melero ◽  
Eugenio Paccagnini ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Binding Protein ◽  
Factor H ◽  
Structural Basis ◽  
Human Monoclonal Antibodies
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