Crystallization of the N-terminal domain of human sex hormone-binding globulin, the major sex steroid carrier in blood
| Autor: | Geoffrey L. Hammond, Gisela Sklenar, Joachim Behlke, Yves A. Muller, David W. Dales, Irina Grishkovskaya, George V. Avvakumov |
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| Rok vydání: | 2000 |
| Předmět: |
Crystallography
X-Ray law.invention Crystal Tetragonal crystal system Sex hormone-binding globulin Protein structure Structural Biology law Sex Hormone-Binding Globulin medicine Escherichia coli Humans Crystallization biology Chemistry General Medicine Peptide Fragments Recombinant Proteins Protein Structure Tertiary Crystallography Sex steroid Dihydrotestosterone biology.protein Ultracentrifuge medicine.drug |
| Zdroj: | Acta crystallographica. Section D, Biological crystallography. 55(Pt 12) |
| ISSN: | 0907-4449 |
| Popis: | The amino-teminal laminin G-like domain of human sex hormone-binding globulin (SHBG), which contains the steroid-binding site and the dimerization domain, has been produced in Escherichia coli, purified to homogeneity and crystallized in complex with 5α-dihydrotestosterone (DHT) in two different crystal forms. Native data sets have been collected for tetragonal crystals (space group P4122 or P4322; unit-cell parameters a = 52.2, c = 148.4 Å) diffracting to 3.3 Å and trigonal crystals (R32; a = 104.0, c = 84.4 Å) diffracting to better than 1.6 Å. Since both crystal forms can only accommodate a single monomer in the asymmetric unit and share twofold rotational symmetry, it is proposed that the homodimer of this truncated form of SHBG, as observed in ultracentrifugation experiments, displays C 2 point-group symmetry. |
| Databáze: | OpenAIRE |
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