2box: Difference between revisions

Revision as of 05:34, 4 April 2013

EGF DOMAINS 1,2,5 OF HUMAN EMR2, A 7-TM IMMUNE SYSTEM MOLECULE, IN COMPLEX WITH STRONTIUM.EGF DOMAINS 1,2,5 OF HUMAN EMR2, A 7-TM IMMUNE SYSTEM MOLECULE, IN COMPLEX WITH STRONTIUM.

FunctionFunction

[EMR2_HUMAN] Cell surface receptor that binds to the chondroitin sulfate moiety of glycosaminoglycan chains and promotes cell attachment. Promotes granulocyte chemotaxis, degranulation and adhesion. In macrophages, promotes the release of inflammatory cytokines, including IL8 and TNF.^[1] ^[2] ^[3]

About this StructureAbout this Structure

2box is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

^{[xtra 1]}^{[xtra 2]}

↑ Abbott RJ, Spendlove I, Roversi P, Fitzgibbon H, Knott V, Teriete P, McDonnell JM, Handford PA, Lea SM. Structural and functional characterization of a novel T cell receptor co-regulatory protein complex, CD97-CD55. J Biol Chem. 2007 Jul 27;282(30):22023-32. Epub 2007 Apr 20. PMID:17449467 doi:M702588200
↑ Abbott RJ, Knott V, Roversi P, Neudeck S, Lukacik P, Handford PA, Lea SM. Crystallization and preliminary X-ray diffraction analysis of three EGF domains of EMR2, a 7TM immune-system molecule. Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):936-8. Epub 2004, Apr 21. PMID:15103144 doi:10.1107/S0907444904005098

↑ Stacey M, Chang GW, Davies JQ, Kwakkenbos MJ, Sanderson RD, Hamann J, Gordon S, Lin HH. The epidermal growth factor-like domains of the human EMR2 receptor mediate cell attachment through chondroitin sulfate glycosaminoglycans. Blood. 2003 Oct 15;102(8):2916-24. Epub 2003 Jun 26. PMID:12829604 doi:10.1182/blood-2002-11-3540
↑ Yona S, Lin HH, Dri P, Davies JQ, Hayhoe RP, Lewis SM, Heinsbroek SE, Brown KA, Perretti M, Hamann J, Treacher DF, Gordon S, Stacey M. Ligation of the adhesion-GPCR EMR2 regulates human neutrophil function. FASEB J. 2008 Mar;22(3):741-51. Epub 2007 Oct 10. PMID:17928360 doi:10.1096/fj.07-9435com
↑ Huang YS, Chiang NY, Hu CH, Hsiao CC, Cheng KF, Tsai WP, Yona S, Stacey M, Gordon S, Chang GW, Lin HH. Activation of myeloid cell-specific adhesion class G protein-coupled receptor EMR2 via ligation-induced translocation and interaction of receptor subunits in lipid raft microdomains. Mol Cell Biol. 2012 Apr;32(8):1408-20. doi: 10.1128/MCB.06557-11. Epub 2012 Feb, 6. PMID:22310662 doi:10.1128/MCB.06557-11

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

[4] Abbott RJ, Spendlove I, Roversi P, Fitzgibbon H, Knott V, Teriete P, McDonnell JM, Handford PA, Lea SM. Structural and functional characterization of a novel T cell receptor co-regulatory protein complex, CD97-CD55. J Biol Chem. 2007 Jul 27;282(30):22023-32. Epub 2007 Apr 20. PMID:17449467 doi:M702588200

[5] Abbott RJ, Knott V, Roversi P, Neudeck S, Lukacik P, Handford PA, Lea SM. Crystallization and preliminary X-ray diffraction analysis of three EGF domains of EMR2, a 7TM immune-system molecule. Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):936-8. Epub 2004, Apr 21. PMID:15103144 doi:10.1107/S0907444904005098

[1] Stacey M, Chang GW, Davies JQ, Kwakkenbos MJ, Sanderson RD, Hamann J, Gordon S, Lin HH. The epidermal growth factor-like domains of the human EMR2 receptor mediate cell attachment through chondroitin sulfate glycosaminoglycans. Blood. 2003 Oct 15;102(8):2916-24. Epub 2003 Jun 26. PMID:12829604 doi:10.1182/blood-2002-11-3540

[2] Yona S, Lin HH, Dri P, Davies JQ, Hayhoe RP, Lewis SM, Heinsbroek SE, Brown KA, Perretti M, Hamann J, Treacher DF, Gordon S, Stacey M. Ligation of the adhesion-GPCR EMR2 regulates human neutrophil function. FASEB J. 2008 Mar;22(3):741-51. Epub 2007 Oct 10. PMID:17928360 doi:10.1096/fj.07-9435com

[3] Huang YS, Chiang NY, Hu CH, Hsiao CC, Cheng KF, Tsai WP, Yona S, Stacey M, Gordon S, Chang GW, Lin HH. Activation of myeloid cell-specific adhesion class G protein-coupled receptor EMR2 via ligation-induced translocation and interaction of receptor subunits in lipid raft microdomains. Mol Cell Biol. 2012 Apr;32(8):1408-20. doi: 10.1128/MCB.06557-11. Epub 2012 Feb, 6. PMID:22310662 doi:10.1128/MCB.06557-11

[1]

[2]

[3]

[xtra 1]

[xtra 2]

@@ Line 1: / Line 1: @@
-[[Image:2box.png|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_2box", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
 {{STRUCTURE_2box|  PDB=2box  |  SCENE=  }}
 ===EGF DOMAINS 1,2,5 OF HUMAN EMR2, A 7-TM IMMUNE SYSTEM MOLECULE, IN COMPLEX WITH STRONTIUM.===
+{{ABSTRACT_PUBMED_17449467}}
+==Function==
-<!--
+[[http://www.uniprot.org/uniprot/EMR2_HUMAN EMR2_HUMAN]] Cell surface receptor that binds to the chondroitin sulfate moiety of glycosaminoglycan chains and promotes cell attachment. Promotes granulocyte chemotaxis, degranulation and adhesion. In macrophages, promotes the release of inflammatory cytokines, including IL8 and TNF.<ref>PMID:12829604</ref> <ref>PMID:17928360</ref> <ref>PMID:22310662</ref>
-The line below this paragraph, {{ABSTRACT_PUBMED_17449467}}, adds the Publication Abstract to the page
-(as it appears on PubMed at http://www.pubmed.gov), where 17449467 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_17449467}}
 ==About this Structure==
@@ Line 22: / Line 10: @@
 ==Reference==
-<ref group="xtra">PMID:017449467</ref><ref group="xtra">PMID:015103144</ref><references group="xtra"/>
+<ref group="xtra">PMID:017449467</ref><ref group="xtra">PMID:015103144</ref><references group="xtra"/><references/>
 [[Category: Homo sapiens]]
 [[Category: Abbott, R J.M.]]
@@ Line 32: / Line 20: @@
 [[Category: Spendlove, I.]]
 [[Category: Teriete, P.]]
+[[Category: 7tm]]
+[[Category: Calcium-binding]]
+[[Category: Cd55]]
+[[Category: Cd97]]
+[[Category: Cell adhesion]]
+[[Category: Egf-like domain]]
+[[Category: G-protein coupled receptor]]
+[[Category: Immune system]]

2box: Difference between revisions

Revision as of 05:34, 4 April 2013

Contents

EGF DOMAINS 1,2,5 OF HUMAN EMR2, A 7-TM IMMUNE SYSTEM MOLECULE, IN COMPLEX WITH STRONTIUM.EGF DOMAINS 1,2,5 OF HUMAN EMR2, A 7-TM IMMUNE SYSTEM MOLECULE, IN COMPLEX WITH STRONTIUM.

FunctionFunction

About this StructureAbout this Structure

ReferenceReference

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

2box: Difference between revisions

Revision as of 05:34, 4 April 2013

EGF DOMAINS 1,2,5 OF HUMAN EMR2, A 7-TM IMMUNE SYSTEM MOLECULE, IN COMPLEX WITH STRONTIUM.EGF DOMAINS 1,2,5 OF HUMAN EMR2, A 7-TM IMMUNE SYSTEM MOLECULE, IN COMPLEX WITH STRONTIUM.

FunctionFunction

About this StructureAbout this Structure

ReferenceReference

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Search