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Crystal structure of the human vascular adhesion protein-1: Unique structural features with functional implications
- Source :
- Protein Science. 14:1964-1974
- Publication Year :
- 2005
- Publisher :
- Wiley, 2005.
-
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.
- Subjects :
- Models, Molecular
Glycosylation
AOC3
Molecular Sequence Data
Crystallography, X-Ray
Biochemistry
Article
Protein structure
Humans
Amino Acid Sequence
Binding site
Molecular Biology
RGD motif
Binding Sites
biology
Chemistry
Cell adhesion molecule
Amine oxidase (copper-containing)
Active site
Adhesion
Protein Structure, Tertiary
biology.protein
Biophysics
Amine Oxidase (Copper-Containing)
Cell Adhesion Molecules
Dimerization
Subjects
Details
- ISSN :
- 1469896X and 09618368
- Volume :
- 14
- Database :
- OpenAIRE
- Journal :
- Protein Science
- Accession number :
- edsair.doi.dedup.....bcf1a4b8447e12faf9af1010a27fdd0f