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Two different crystal forms of sorcin, a penta-EF-hand Ca2+-binding protein (2001)

Nastopoulos, Vassilios ; Ilari, Andrea ; Colotti, Gianni ; [et al.]

Copenhagen : International Union of Crystallography (IUCr)

Acta crystallographica 57 (2001), S. 862-864

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ISSN: 1399-0047

Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001

Topics: Chemistry and Pharmacology , Geosciences , Physics

Notes: Sorcin is a 198 amino-acid Ca2+-binding protein that belongs to the penta-EF-hand family. Its Ca2+-binding domain (residues 33–198) has been crystallized in the absence of Ca2+ in two different crystal forms. Two complete data sets have been collected on a synchrotron source under cryocooling conditions from crystals grown using ammonium sulfate as precipitant: monoclinic crystals in space group C2, with unit-cell parameters a = 130.93, b = 103.85, c = 78.55 Å, β = 118.0°, diffracting to 2.1 Å, and tetragonal crystals in space group P4212, with unit-cell parameters a = b = 103.33, c = 79.15, diffracting to 2.7 Å. Crystals were also grown using PEG 6000 as precipitating agent. They also belong to space group C2, diffract to 2.8 Å and their unit-cell parameters are very similar to the first form. Structure determination by molecular replacement has been initiated. Structural information should be useful for elucidating the interaction of sorcin with membrane targets.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1107/S0907444901004553

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Expression and localisation of annexin VII (synexin) isoforms in differentiating myoblasts (1999)

Clemen, Christoph S. ; Hofmann, Andreas ; Zamparelli, Carlotta ; [et al.]

Springer

Journal of muscle research and cell motility 20 (1999), S. 669-679

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ISSN: 1573-2657

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine

Notes: Abstract Annexin VII exists in a 47 kDa and a 51 kDa isoform with the 51 kDa protein being the only isoform present in skeletal muscle. Expression of the 51 kDa isoform during myogenesis and localization was studied in cells after conversion into myogenic cells by transduction with MyoD and in mouse and human myogenic cell lines. MyoD expression in NIH3T3 and C3H10T1/2 fibroblasts led to disappearance of the mRNA specific for the 47kDa isoform and appearance of the 51 kDa isoform-specific mRNA. The overall amount of annexin VII protein was reduced in myogenic converted cells. Both in undifferentiated and differentiated cells annexin VII was localized by immunofluorescence microscopy to punctate structures which were distributed all over the cell. A GFP annexin VII fusion protein showed a similar distribution. Cell fractionation studies indicated that annexin VII is equally distributed between cytosol and membrane fractions in undifferentiated cells, while in differentiated cells it is exclusively present in the membrane fraction. By sucrose gradient centrifugation of postnuclear supernatants we identified two distinct annexin VII-containing membrane populations that cofractionated with caveolin 3- and sorcin-containing membranes.