X-ray diffraction analysis of glycoprotein D from herpes simplex virus type 2 / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 1499-1506, 2011.
Article
in English
| WPRIM
| ID: wpr-304552
ABSTRACT
Glycoprotein D (gD) of Herpes simplex virus type 2 (HSV-2) is a key factor mediating the entry of HSV-2 into host cells. In order to explain the mechanism underlying the gD-mediated receptor-binding and viral entry, we performed a structural study on HSV-2 gD. The ectodomain of the gD protein encompassing residues 1 to 285 was expressed by baculovirus-infected insect cells as a secreted soluble protein with a C-terminal hexa-his tag. The protein was then purified by affinity and size-exclusion chromatography. The purified protein was successfully crystallized using the hanging-drop vapor-diffusion at 18 degrees C in a condition consisting of 0.1 mol/L Hepes pH 7.2, 5% (V/V) 2-methyl-2,4-pentanediol (MPD) and 10% PEG 10 000. The crystals diffracted to 1.8 angstroms resolution and belonged to space group P21, with unit-cell parameters alpha = 63.6, b = 55.4, c = 65.3 angstroms, beta = 96.3 degrees.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Recombinant Proteins
/
Chemistry
/
Viral Fusion Proteins
/
Baculoviridae
/
Herpesvirus 2, Human
/
Crystallography, X-Ray
/
Crystallization
/
Genetics
/
Insecta
/
Metabolism
Limits:
Animals
Language:
English
Journal:
Chinese Journal of Biotechnology
Year:
2011
Type:
Article
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