3ala

From Proteopedia

(Difference between revisions)

Current revision

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

Structural highlights

3ala is a 7 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.9Å
Ligands:	, , , , , , ,
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.

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ala"

Categories: Homo sapiens | Large Structures | Ernberg KE | Guss JM | McGrath AP

@@ Line 1: / Line 1: @@
-[[Image:3ala.png|left|200px]]
-<!--
+==Crystal structure of vascular adhesion protein-1 in space group C2==
-The line below this paragraph, containing "STRUCTURE_3ala", creates the "Structure Box" on the page.
+<StructureSection load='3ala' size='340' side='right'caption='[[3ala]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3ala]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ALA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ALA FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TPQ:5-(2-CARBOXY-2-AMINOETHYL)-2-HYDROXY-1,4-BENZOQUINONE'>TPQ</scene></td></tr>
-{{STRUCTURE_3ala|  PDB=3ala  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ala FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ala OCA], [https://pdbe.org/3ala PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ala RCSB], [https://www.ebi.ac.uk/pdbsum/3ala PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ala ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/AOC3_HUMAN 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.<ref>PMID:9653080</ref> <ref>PMID:17400359</ref> <ref>PMID:19588076</ref>
+<div style="background-color:#fffaf0;">
+== 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.
-===Crystal structure of vascular adhesion protein-1 in space group C2===
+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<ref>PMID:21139198</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_21139198}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 3ala" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 21139198 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_21139198}}
-==About this Structure==
-[[3ala]] is a 7 chain structure of [[Copper Amine Oxidase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ALA OCA].
 ==See Also==
-*[[Copper Amine Oxidase|Copper Amine Oxidase]]
+*[[Copper amine oxidase 3D structures|Copper amine oxidase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:021139198</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Primary-amine oxidase]]
+[[Category: Large Structures]]
-[[Category: Ernberg, K E.]]
+[[Category: Ernberg KE]]
-[[Category: Guss, J M.]]
+[[Category: Guss JM]]
-[[Category: McGrath, A P.]]
+[[Category: McGrath AP]]
-[[Category: Copper containing amine oxidase]]
-[[Category: Membrane primary amine oxidase]]
-[[Category: Oxidoreductase]]
-[[Category: Semicarbazide-sensitive amine oxidase]]
-[[Category: Ssao]]
-[[Category: Vap-1]]
-[[Category: Vascular adhesion protein-1]]

3ala

From Proteopedia

Current revision

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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