Crystal structure of chicken riboflavin-binding protein

The X-ray crystal structure of the dimerized atrial natriuretic factor (ANF) receptor hormone-binding domain has provided a first structural view of this anti-hypertensive receptor. The structure reveals a surprising evolutionary link to the periplasmic-binding protein fold family. Furthermore, the presence of a chloride ion in the membrane distal domain and the presence of a second putative effector pocket suggests that the extracellular domain of this receptor is allosterically regulated. The scope of this article is to extensively review the data published on this receptor and to correlate it with the hormone-binding domain structure. In addition, a more detailed description is provided of the important features of this structure including the different binding sites for the ANF hormone, chloride ion, putative effector pocket, glycosylation sites, and dimer interface.Key words: crystal structure, periplasmic-binding protein fold, guanylyl cyclase, hormone receptor.

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Crystal Structure of Thaumatin I, a Sweet Taste Receptor Binding Protein

Crystallography in Molecular Biology ◽

10.1007/978-1-4684-5272-3_36 ◽

1987 ◽

pp. 395-402

Author(s):

Abraham de Vos ◽

Sung-Hou Kim

Keyword(s):

Crystal Structure ◽

Receptor Binding ◽

Binding Protein ◽

Taste Receptor ◽

Sweet Taste ◽

Sweet Taste Receptor ◽

Receptor Binding Protein

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Crystal structure of prokaryotic ribosomal protein L9: a bi-lobed RNA-binding protein.

The EMBO Journal ◽

10.1002/j.1460-2075.1994.tb06250.x ◽

1994 ◽

Vol 13 (1) ◽

pp. 205-212 ◽

Cited By ~ 72

Author(s):

D.W. Hoffman ◽

C. Davies ◽

S.E. Gerchman ◽

J.H. Kycia ◽

S.J. Porter ◽

...

Keyword(s):

Crystal Structure ◽

Ribosomal Protein ◽

Rna Binding ◽

Binding Protein ◽

Rna Binding Protein ◽

Ribosomal Protein L9

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The Crystal Structure ofHelicobacter pyloriCysteine-rich Protein B Reveals a Novel Fold for a Penicillin-binding Protein

Journal of Biological Chemistry ◽

10.1074/jbc.m108993200 ◽

2002 ◽

Vol 277 (12) ◽

pp. 10187-10193 ◽

Cited By ~ 30

Author(s):

Lucas Lüthy ◽

Markus G. Grütter ◽

Peer R. E. Mittl

Keyword(s):

Crystal Structure ◽

Binding Protein ◽

Penicillin Binding Protein ◽

Protein B

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

Nucleic Acids Research ◽

10.1093/nar/gkaa076 ◽

2020 ◽

Vol 48 (6) ◽

pp. 3356-3365 ◽

Cited By ~ 4

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.

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