PMID: 16046623

 

    Legend: Gene, Sites

Title : Crystal structure of the human vascular adhesion protein-1 : unique structural features with functional implications

Abstract :

1. 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
2. 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
3. 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
4. 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
5. Secondly, sugar units are clearly observed at two of the six predicted N-glycosylation sites
6. Moreover, mutagenesis analysis showed that all of the predicted sites were glycosylated in the protein used for crystallization
7. 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

Output (sent_index, trigger, protein, sugar, site):

• 5. N-glycosylation, , -, -, sites
• 5. observed, , -, sugar units, sites
• 6. glycosylated, , -, -, sites
• 6. glycosylated, , -, all, sites
• 6. glycosylated, , protein, -, sites
• 6. glycosylated, , protein, all, -

Output(Part-Of) (sent_index, protein, site):

• 4. channel, Leu469

*Output_Site_Fusion* (sent_index, protein, sugar, site):

 

Protein	NCBI ID	SENTENCE INDEX
CAO	8639	2