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

被引：13

作者：

Grishkovskaya, I

Sklenar, G

Avvakumov, GV

Dales, D

Behlke, J

Hammond, GL

Muller, YA ^{[1
]}

机构：

[1] Max Delbruck Ctr Mol Med, Forsch Grp Kristallog, D-13092 Berlin, Germany

[2] Univ Western Ontario, MRC, Grp Fetal & Neonatal Hlth & Dev, Dept Obstet & Gynaecol, London, ON N6A 4L6, Canada

[3] Univ Western Ontario, MRC, Grp Fetal & Neonatal Hlth & Dev, Dept Pharmacol & Toxicol, London, ON N6A 4L6, Canada

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1999年 / 55卷

关键词：

D O I：

10.1107/S0907444999012883

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 Sa-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 Angstrom) diffracting to 3.3 Angstrom and trigonal crystals (R32; a = 104.0, c = 84.4 Angstrom) diffracting to better than 1.6 Angstrom. 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.

引用

页码：2053 / 2055

页数：3

共 10 条

[1] Merging extracellular domains: Fold prediction for laminin G-like and amino-terminal thrombospondin-like modules based on homology to pentraxins [J].