| Structural highlights
3ala is a 7 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , , , , |
| NonStd Res: | |
| Related: | 2c10, 1pu4, 1us1, 2c11 |
| Gene: | AOC3, VAP1 (HUMAN) |
| Activity: | Primary-amine oxidase, with EC number 1.4.3.21 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[AOC3_HUMAN] Cell adhesion protein that participates in lymphocyte recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion. Has a monoamine oxidase activity. May play a role in adipogenesis.[1] [2] [3]
Publication Abstract from PubMed
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 A, beta=112.3 degrees . The structure was refined to a resolution of 2.9 A, with Rcryst and Rfree values of 0.250 and 0.286, respectively.
A new crystal form of human vascular adhesion protein 1.,Ernberg K, McGrath AP, Peat TS, Adams TE, Xiao X, Pham T, Newman J, McDonald IA, Collyer CA, Guss JM Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Dec 1;66(Pt, 12):1572-8. Epub 2010 Nov 16. PMID:21139198[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Smith DJ, Salmi M, Bono P, Hellman J, Leu T, Jalkanen S. Cloning of vascular adhesion protein 1 reveals a novel multifunctional adhesion molecule. J Exp Med. 1998 Jul 6;188(1):17-27. PMID:9653080
- ↑ Bour S, Daviaud D, Gres S, Lefort C, Prevot D, Zorzano A, Wabitsch M, Saulnier-Blache JS, Valet P, Carpene C. Adipogenesis-related increase of semicarbazide-sensitive amine oxidase and monoamine oxidase in human adipocytes. Biochimie. 2007 Aug;89(8):916-25. Epub 2007 Feb 24. PMID:17400359 doi:http://dx.doi.org/10.1016/j.biochi.2007.02.013
- ↑ Kaitaniemi S, Elovaara H, Gron K, Kidron H, Liukkonen J, Salminen T, Salmi M, Jalkanen S, Elima K. The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase. Cell Mol Life Sci. 2009 Aug;66(16):2743-57. doi: 10.1007/s00018-009-0076-5. Epub , 2009 Jul 9. PMID:19588076 doi:http://dx.doi.org/10.1007/s00018-009-0076-5
- ↑ Ernberg K, McGrath AP, Peat TS, Adams TE, Xiao X, Pham T, Newman J, McDonald IA, Collyer CA, Guss JM. A new crystal form of human vascular adhesion protein 1. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Dec 1;66(Pt, 12):1572-8. Epub 2010 Nov 16. PMID:21139198 doi:10.1107/S1744309110041515
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