0000000000480853

AUTHOR

Patrick Scheerer

0000-0001-5028-2075

showing 2 related works from this author

Insights into functional aspects of centrins from the structure of N-terminally extended mouse centrin 1

2006

AbstractCentrins are members of the family of Ca2+-binding EF-hand proteins. In photoreceptor cells, centrin isoform 1 is specifically localized in the non-motile cilium. This connecting cilium links the light-sensitive outer segment with the biosynthetic active inner segment of the photoreceptor cell. All intracellular exchanges between these compartments have to occur through this cilium. Three-dimensional structures of centrins from diverse organisms are known, showing that the EF-hand motifs of the N-terminal domains adopt closed conformations, while the C-terminal EF-hand motifs have open conformations. The crystal structure of an N-terminally extended mouse centrin 1 (MmCen1-L) resemb…

Protein ConformationAmino Acid MotifsSequence HomologyPlasma protein bindingEF-handTroponin CMiceStructure-Activity RelationshipProtein structureCalcium-binding proteinConnecting ciliumCentrinAnimalsHumansPhotoreceptor CellsCiliaEF Hand MotifsProtein Structure QuaternaryChemistryEF handCiliumCalcium-Binding ProteinsTerminal Repeat SequencesCalcium-binding proteinSensory SystemsProtein Structure TertiaryCell biologyOphthalmologyCentrinCalciumTransducinsense organsX-ray structureProtein BindingVision Research
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Crystallization and preliminary X-ray studies of mouse centrin1.

2005

The expression, purification, crystallization and preliminary X-ray diffraction studies of mouse centrin1 are reported. Centrins belong to a family of Ca{sup 2+}-binding EF-hand proteins that play a fundamental role in centrosome duplication and the function of cilia. To shed light on the structure–function relationship of these proteins, mouse centrin1 has been crystallized. The mouse centrin1 has been expressed in Escherichia coli as a GST-centrin fusion protein containing a thrombin protease cleavage site between the fusion partners. Two constructs with different linking-sequence lengths were expressed and purified. Thrombin cleavage yielded functional centrin1 and N-terminally extended …

StereochemistryChromosomal Proteins Non-HistoneMolecular Sequence DataBiophysicsmacromolecular substancesCleavage (embryo)Crystallography X-RayBiochemistrylaw.inventionchemistry.chemical_compoundMiceStructure-Activity RelationshipThrombinStructural BiologylawGeneticsmedicineEscherichia coliAnimalsCentrosome duplicationAmino Acid SequenceCrystallizationDose-Response Relationship DrugCalcium-Binding ProteinsSpace groupCondensed Matter PhysicsFusion proteinRecombinant ProteinsCrystallographyenzymes and coenzymes (carbohydrates)KineticschemistryCrystallization CommunicationsX-ray crystallographybiological scienceshealth occupationsbacteriaCrystallizationEthylene glycolmedicine.drugActa crystallographica. Section F, Structural biology and crystallization communications
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