0000000000367874

AUTHOR

Oliviero Carugo

showing 2 related works from this author

Metal complexes of the carbonic anhydrase inhibitor methazolamide (Hmacm). Crystal structure of the Zn(macm)2 (NH3)2. Anticonvulsant properties of th…

1995

Complexes of Co(II), Cu(II), and Zn(II) with deprotonated methazolamide and ammonia are synthesized and characterized. The complex Zn(macm)2(NH3)2 crystallizes in the monoclinic C2/c space group with a = 13.468(1), b = 6.759(1), c = 23.014(2) A, beta = 90.27(1), and Z = 4. The structure was refined to R = 0.049 (Rw = 0.053). The Zn(II) ion is coordinated to two deprotonated sulfonamido nitrogen atoms of the macm- ligand and two nitrogen atoms of the ammonia ligands in a distorted tetrahedron. The Zn(macm)2(NH3)2 complex is shown to be a simple model for the methazolamide inhibition of CA. EHMO calculations applied to fractional coordinates of the Zn(macm)2(NH3)2 complex indicate that the at…

Spectrophotometry InfraredCations DivalentInorganic chemistryMethazolamidechemistry.chemical_elementCrystal structureZincCrystallography X-RayBiochemistryInorganic ChemistryMetalDeprotonationmedicineAnimalsMethazolamideHOMO/LUMOMolecular StructureChemistryLigandElectron Spin Resonance SpectroscopyCobaltZincCrystallographyvisual_artvisual_art.visual_art_mediumAnticonvulsantsCoppermedicine.drugMonoclinic crystal systemJournal of Inorganic Biochemistry
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Crystal Structure of Human Filamin C Domain 23 and Small Angle Scattering Model for Filamin C 23–24 Dimer

2007

Filamin C is a dimeric, actin-binding protein involved in organization of cortical cytoskeleton and of the sarcomere. We performed crystallographic, small-angle X-ray scattering and analytical ultracentrifugation experiments on the constructs containing carboxy-terminal domains of the protein (domains 23-24 and 19-21). The crystal structure of domain 23 of filamin C showed that the protein adopts the expected immunoglobulin (Ig)-like fold. Small-angle X-ray scattering experiments performed on filamin C tandem Ig-like domains 23 and 24 reveal a dimer that is formed by domain 24 and that domain 23 has little interactions with itself or with domain 24, while the analytical ultracentrifugation …

Models MolecularProtein FoldingFilaminsDimermacromolecular substancesCrystal structureCrystallography X-RayFilaminSarcomereAnalytical Ultracentrifugationchemistry.chemical_compoundContractile ProteinsNickelStructural BiologyScattering Small AngleHumansMolecular BiologyBinding SitesSmall-angle X-ray scatteringScatteringMicrofilament ProteinsProtein Structure TertiaryCrystallographychemistrySmall-angle scatteringDimerizationUltracentrifugationJournal of Molecular Biology
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