Crystallization and preliminary X-ray analysis of the human vascular adhesion protein-1

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 59; no. 7; pp. 1288 - 1290
• Main Authors: Nymalm, Yvonne, Kidron, Heidi, Söderholm, Annu, Viitanen, Lenita, Kaukonen, Kimmo, Pihlavisto, Marjo, Smith, David, Veromaa, Timo, Airenne, Tomi T., Johnson, Mark S., Salminen, Tiina A.
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England Munksgaard International Publishers 01.07.2003
• Subjects: adhesion molecules; Amine Oxidase (Copper-Containing) - chemistry; Amine Oxidase (Copper-Containing) - isolation & purification; amine oxidases; Cell Adhesion Molecules - chemistry; Cell Adhesion Molecules - isolation & purification; Cloning, Molecular; Crystallization; Glycosylation; Humans; membrane proteins; Recombinant Proteins; topaquinone; VAP-1; X-Ray Diffraction
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S090744490300979X

Human vascular adhesion protein‐1 (VAP‐1) is a membrane‐bound multifunctional glycoprotein with both adhesive and enzymatic properties. The protein belongs to the copper‐containing amine oxidase (CAO) family, which use 2,4,5‐trihydroxyphenylalanine quinone as a cofactor. Here, the crystallization and preliminary X‐­ray analysis of a mammalian CAO, human VAP‐1, is reported. The protein was expressed in Chinese hamster ovary cells as a full‐length form with an N‐terminal transmembrane region and multiple glycosylation sites. Hexagonal crystals with unit‐cell parameters a = b = 225.9, c = 218.7 Å, α = β = 90, γ = 120° were obtained using the vapour‐diffusion method. Data from three different crystals were collected at 100 K using synchrotron radiation and were processed to 3.2 Å resolution with 95.9% completeness and an Rmerge of 19.6%.