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

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.

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Purification, crystallization and preliminary X-ray analysis of catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa

Acta Crystallographica Section D Biological Crystallography ◽

10.1107/s0907444999007970 ◽

1999 ◽

Vol 55 (9) ◽

pp. 1591-1593 ◽

Cited By ~ 1

Author(s):

G. Sainz ◽

J. Vicat ◽

R. Kahn ◽

C. Tricot ◽

V. Stalon ◽

...

Keyword(s):

Pseudomonas Aeruginosa ◽

Point Group ◽

Unit Cell ◽

Group Symmetry ◽

Ornithine Carbamoyltransferase ◽

Unit Cell Parameters ◽

Crystal Forms ◽

Space Group ◽

Cell Parameters ◽

Hexagonal Crystals

The catabolic ornithine carbamoyltransferase (OTCase) from Pseudomonas aeruginosa exhibits allosteric behaviour, with two conformational states of the molecule: an active R form and an inactive T form. The enzyme is a dodecamer with a molecular mass of 455700 Da. Three crystal forms have been obtained. Crystals of allosteric state T are rhombohedral, belonging to the R3 space group, with hexagonal unit-cell parameters a = b = 180.6, c = 122.0 Å. They diffract to a resolution of 4.5 Å. Two crystal forms for allosteric state R have been obtained, with hexagonal and cubic symmetries. Hexagonal crystals, which diffract to a resolution of 3.4 Å, belong to the space group P63 with unit-cell parameters a = b = 140.8, c = 145.6 Å. The cubic crystals belong to space group I23, with unit-cell parameter a = 134.32 Å and diffract to a resolution better than 2.5 Å. In all crystal forms, the dodecamer exhibits a 23 point-group symmetry.

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Use Sex Hormone-Binding Globulin as Screen for PCOS

Skin & Allergy News ◽

10.1016/s0037-6337(05)70234-5 ◽

2005 ◽

Vol 36 (5) ◽

pp. 40

Author(s):

PATRICE WENDLING

Keyword(s):

Sex Hormone ◽

Sex Hormone Binding Globulin ◽

Hormone Binding

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Effects of oestradiol on sex hormone binding globulin

Acta Endocrinologica ◽

10.1530/acta.0.1010248 ◽

1982 ◽

Vol 101 (2) ◽

pp. 248-253 ◽

Cited By ~ 36

Author(s):

Viveca Odlind ◽

Kerstin Elamsson ◽

Doris E. Englund ◽

Arne Victor ◽

Elof D. B. Johansson

Keyword(s):

Luteal Phase ◽

Sex Hormone ◽

Sex Hormone Binding Globulin ◽

Hormone Binding ◽

Pronounced Increase ◽

Menstrual Cycles ◽

Menopausal Women ◽

Plasma Oestradiol

Abstract. Sex hormone binding globulin (SHBG) levels were studied for possible effects of oestradiol-17β on SHBG. No change in SHBG plasma was recorded during normal menstrual cycles or during treatment with oestradiol-17β to menopausal women. However, gonadotrophin treatment to amenorrhoeic women to induce ovulation resulted in high oestradiol concentrations and a pronounced increase in SHBG was found during the luteal phase of these cycles. A marked increase of SHBG was also recorded in a woman with pronounced fluctuations of oestradiol during treatment with levonorgestrel sc implants for contraception. In conclusion, effects on SHBG were only found when extraordinarily high levels of plasma oestradiol were recorded.

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