1US1

Crystal structure of human vascular adhesion protein-1

Summary for 1US1

• Entry DOI: 10.2210/pdb1us1/pdb
• Descriptor: MEMBRANE COPPER AMINE OXIDASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, COPPER (II) ION, ... (5 entities in total)
• Functional Keywords: oxidase, copper amine oxidase, vascular adhesion protein-1
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cell membrane ; Single-pass type II membrane protein : Q16853
• Total number of polymer chains: 2
• Total formula weight: 171047.75

Authors

Airenne, T.T.,Nymalm, Y.,Kidron, H.,Soderholm, A.,Johnson, M.S.,Salminen, T.A. (deposition date: 2003-11-17, release date: 2005-02-16, Last modification date: 2023-12-13)

Primary citation

Airenne, T.T.,Nymalm, Y.,Kidron, H.,Smith, D.J.,Pihlavisto, M.,Salmi, M.,Jalkanen, S.,Johnson, M.S.,Salminen, T.A.
Crystal Structure of the Human Vascular Adhesion Protein-1: Unique Structural Features with Functional Implications.
Protein Sci., 14:1964-, 2005

PubMed Abstract: The expression of human vascular adhesion protein-1 (hVAP-1) is induced at sites of inflammation where extravasation of lymphocytes from blood to the peripheral tissue occurs. We have solved the X-ray structure of hVAP-1, a human copper amine oxidase (CAO), which is distinguished from other CAOs in being membrane-bound. The dimer structure reveals some intriguing features that may have fundamental roles in the adhesive and enzymatic functions of hVAP-1, especially regarding the role of hVAP-1 in inflammation, lymphocyte attachment, and signaling. Firstly, Leu469 at the substrate channel may play a key role in controlling the substrate entry; depending on its conformation, it either blocks or gives access to the active site. Secondly, sugar units are clearly observed at two of the six predicted N-glycosylation sites. Moreover, mutagenesis analysis showed that all of the predicted sites were glycosylated in the protein used for crystallization. Thirdly, the existence of a solvent-exposed RGD motif at the entrance to each active site in hVAP-1 suggests that it may have a functional role.

PubMed: 16046623
DOI: 10.1110/PS.051438105

Experimental method

X-RAY DIFFRACTION (2.9 Å)