3ALA

Crystal structure of vascular adhesion protein-1 in space group C2

Summary for 3ALA

• Entry DOI: 10.2210/pdb3ala/pdb
• Related: 1pu4 1us1 2c10 2c11
• Descriptor: Membrane primary amine oxidase, 2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (11 entities in total)
• Functional Keywords: membrane primary amine oxidase, vascular adhesion protein-1, vap-1, semicarbazide-sensitive amine oxidase, ssao, copper containing amine oxidase, oxidoreductase
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type II membrane protein: Q16853
• Total number of polymer chains: 7
• Total formula weight: 595576.36

Authors

Ernberg, K.E.,McGrath, A.P.,Guss, J.M. (deposition date: 2010-07-29, release date: 2010-12-15, Last modification date: 2023-11-01)

Primary citation

Ernberg, K.,McGrath, A.P.,Peat, T.S.,Adams, T.E.,Xiao, X.,Pham, T.,Newman, J.,McDonald, I.A.,Collyer, C.A.,Guss, J.M.
A new crystal form of human vascular adhesion protein 1
Acta Crystallogr.,Sect.F, 66:1572-1578, 2010

PubMed Abstract: Human vascular adhesion protein 1 (VAP-1) is involved in lymphocyte-endothelial cell adhesion and has been implicated in many human inflammatory diseases. VAP-1 is a member of the copper amine oxidase family of enzymes with a trihydroxyphenylalanine quinone (TPQ) cofactor. Previously characterized crystals of VAP-1 suffered from anisotropy and contained disordered regions; in addition, one form was consistently twinned. In an effort to grow crystals that diffracted to higher resolution for inhibitor-binding studies, a construct with an N-terminal deletion was made and expressed in the Chinese hamster ovary (CHO) glycosylation mutant cell line Lec8. Screening produced crystals that displayed some anisotropy and contained seven molecules per asymmetric unit. These crystals belonged to space group C2, with unit-cell parameters a=394.5, b=115.8, c=179.3 Å, β=112.3°. The structure was refined to a resolution of 2.9 Å, with Rcryst and Rfree values of 0.250 and 0.286, respectively.

PubMed: 21139198
DOI: 10.1107/S1744309110041515

Experimental method

X-RAY DIFFRACTION (2.9 Å)