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Crystallization of the N-terminal domain of human sex hormone-binding globulin, the major sex steroid carrier in blood

Item Type:Article
Title:Crystallization of the N-terminal domain of human sex hormone-binding globulin, the major sex steroid carrier in blood
Creators Name:Grishkovskaya, I. and Sklenar, G. and Avvakumov, G.V. and Dales, D. and Behlke, J. and Hammond, G.L. and Muller, Y.A.
Abstract: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 5alpha-dihydrotestosterone (DHT) in two different crystal forms. Native data sets have been collected for tetragonal crystals (space group P4(1)22 or P4(3)22; unit-cell parameters a = 52.2, c = 148.4 A) diffracting to 3.3 A and trigonal crystals (R32; a = 104.0, c = 84.4 A) diffracting to better than 1.6 A. 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.
Keywords:Globulins, Sex Hormones, Steroid Carriers
Source:Acta Crystallographica Section D
ISSN:0907-4449
Publisher:International Union of Crystallography (U.K.)
Volume:55
Number:Pt 12
Page Range:2053-2055
Date:December 1999
Official Publication:http://onlinelibrary.wiley.com/doi/10.1107/S0907444999012883/abstract
PubMed:View item in PubMed

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