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Crystallization and preliminary X-ray crystallographic studies of the PDZ domain of Shank1 from Rattus norvegicus

Shank proteins are a new family of scaffold proteins interacting with various membrane and cytoplasmic proteins. Shank contains multiple protein–protein interaction sites, including ankyrin repeats, an SH3 domain, a PDZ domain, a long proline‐rich region and an SAM domain. The PDZ domain of Shank bi...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2002-08, Vol.58 (8), p.1353-1355
Main Authors: Park, Seong Ho, Im, Young Jun, Rho, Seong-Hwan, Lee, Jun Hyuck, Yang, Soyoung, Kim, Eunjoon, Eom, Soo Hyun
Format: Article
Language:English
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Summary:Shank proteins are a new family of scaffold proteins interacting with various membrane and cytoplasmic proteins. Shank contains multiple protein–protein interaction sites, including ankyrin repeats, an SH3 domain, a PDZ domain, a long proline‐rich region and an SAM domain. The PDZ domain of Shank binds to the C‐terminus of guanylate kinase‐associated protein (GKAP). The PDZ domain of Shank1 from Rattus norvegicus and its complex with the C‐terminal octapeptide of GKAP were crystallized at 294 K using polyethylene glycol 20 000 and 6000 as precipitants. Diffraction data sets from a peptide‐free crystal and a complex crystal were collected to 1.8 and 3.2 Å resolution, respectively, using synchrotron radiation. The peptide‐free crystal belongs to space group P21, with unit‐cell parameters a = 42.0, b = 50.3, c = 51.8 Å, β = 106.3°. The complex crystal belongs to space group P212121, with unit‐cell parameters a = 89.4, b = 97.5, c = 108.3 Å.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444902009162