Journal ArticleDOI
Predicting coiled coils from protein sequences
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TLDR
This method was used to delineate coiled-coil domains in otherwise globular proteins, such as the leucine zipper domains in transcriptional regulators, and to predict regions of discontinuity within coiled -coil structures,such as the hinge region in myosin.Abstract:
The probability that a residue in a protein is part of a coiled-coil structure was assessed by comparison of its flanking sequences with sequences of known coiled-coil proteins. This method was used to delineate coiled-coil domains in otherwise globular proteins, such as the leucine zipper domains in transcriptional regulators, and to predict regions of discontinuity within coiled-coil structures, such as the hinge region in myosin. More than 200 proteins that probably have coiled-coil domains were identified in GenBank, including alpha- and beta-tubulins, flagellins, G protein beta subunits, some bacterial transfer RNA synthetases, and members of the heat shock protein (Hsp70) family.read more
Citations
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Disease-causing mutations within the lysosomal integral membrane protein type 2 (LIMP-2) reveal the nature of binding to its ligand β-glucocerebrosidase
TL;DR: It is demonstrated that disruption of the coiled-coil structure or AMRF disease-causing mutations abolish beta-GC binding, indicating the importance of an intact coiled and amphiphatic structure for the interaction of LIMP-2 and beta- GC.
Journal ArticleDOI
Alternative splicing converts STIM2 from an activator to an inhibitor of store-operated calcium channels
Anshul Rana,Michelle Yen,Amir M. Sadaghiani,Seth Malmersjö,Chan Young Park,Ricardo E. Dolmetsch,Ricardo E. Dolmetsch,Richard S. Lewis +7 more
TL;DR: STIM2β is a novel STIM2 splice isoform that inhibits Orai channels and could lead to novel drugs to treat central giant cell granuloma.
Journal ArticleDOI
Coiled‐coil proteins associated with type III secretion systems: a versatile domain revisited
Robin M. Delahay,Gad Frankel +1 more
TL;DR: Coiled-coils are ubiquitous and highly versatile assembly motifs found in a wide range of structural and regulatory proteins, and evidence accumulating from functional studies suggests an intrinsic involvement of coiled-cils in subunit assembly, translocation and flexible interactions with multiple bacterial and host proteins.
Journal ArticleDOI
Functional analysis of the glaucoma-causing TIGR/myocilin protein: Integrity of amino-terminal coiled-coil regions and olfactomedin homology domain is essential for extracellular adhesion and secretion
TL;DR: It is demonstrated that intracellular sequestration might be the primary mechanism contributing to myocilin-related POAG as it was associated with more than 80% of the disease-causing mutants tested in the authors' study.
Journal ArticleDOI
Characterization of KIFC2, a Neuronal Kinesin Superfamily Member in Mouse
TL;DR: The cloned and characterized KIFC2, a novel kinesin superfamily member from mouse brain, suggest that, unlike other C-terminal motor proteins that appear to be involved in cell division, KI FC2 may play a role in retrograde axonal transport.
References
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Journal ArticleDOI
The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins
TL;DR: A 30-amino-acid segment of C/EBP, a newly discovered enhancer binding protein, shares notable sequence similarity with a segment of the cellular Myc transforming protein, and may represent a characteristic property of a new category of DNA binding proteins.
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Evidence that the leucine zipper is a coiled coil
TL;DR: A peptide corresponding to the leucine zipper region of the yeast transcriptional activator GCN4 was synthesized and characterized and associates in the micromolar concentration range to form a very stable dimer of alpha helices with a parallel orientation.
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Cyclic AMP-responsive DNA-binding protein: structure based on a cloned placental cDNA.
TL;DR: The putative DNA-binding domain of CREB is structurally similar to the corresponding domains in the phorbol ester-responsive c-jun protein and the yeast transcription factor GCN4.
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α‐Helical coiled coils and bundles: How to design an α‐helical protein
Carolyn Cohen,David A.D. Parry +1 more
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A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A.
TL;DR: The three-dimensional crystal structure of seryl-transfer RNA synthetase from Escherichia coli, refined at 2.5 Å resolution, is described, and is the first representative of a second class of aminoacyl-tRNA synthet enzyme structures.