1nbq

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[[Image:1nbq.jpg|left|200px]]
 
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{{Structure
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==Crystal Structure of Human Junctional Adhesion Molecule Type 1==
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|PDB= 1nbq |SIZE=350|CAPTION= <scene name='initialview01'>1nbq</scene>, resolution 2.90&Aring;
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<StructureSection load='1nbq' size='340' side='right'caption='[[1nbq]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1nbq]] is a 2 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=1NBQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NBQ FirstGlance]. <br>
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|ACTIVITY=
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</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>
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|GENE= JAM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nbq OCA], [https://pdbe.org/1nbq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nbq RCSB], [https://www.ebi.ac.uk/pdbsum/1nbq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nbq ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nbq OCA], [http://www.ebi.ac.uk/pdbsum/1nbq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nbq RCSB]</span>
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[https://www.uniprot.org/uniprot/JAM1_HUMAN JAM1_HUMAN] Seems to play a role in epithelial tight junction formation. Appears early in primordial forms of cell junctions and recruits PARD3. The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly (By similarity). Plays a role in regulating monocyte transmigration involved in integrity of epithelial barrier. Involved in platelet activation. In case of orthoreovirus infection, serves as receptor for the virus.
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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'''Crystal Structure of Human Junctional Adhesion Molecule Type 1'''
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nb/1nbq_consurf.spt"</scriptWhenChecked>
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==Overview==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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Reovirus attachment to cells is mediated by the binding of viral attachment protein sigma 1 to junctional adhesion molecule 1 (JAM1). The crystal structure of the extracellular region of human JAM1 (hJAM1) reveals two concatenated Ig-type domains with a pronounced bend at the domain interface. Two hJAM1 molecules form a dimer that is stabilized by extensive ionic and hydrophobic contacts between the N-terminal domains. This dimeric arrangement is similar to that observed previously in the murine homolog of JAM1, indicating physiologic relevance. However, differences in the dimeric structures of hJAM1 and murine JAM1 suggest that the interface is dynamic, perhaps as a result of its ionic nature. We demonstrate that hJAM1, but not the related proteins hJAM2 and hJAM3, serves as a reovirus receptor, which provides insight into sites in hJAM1 that likely interact with sigma 1. In addition, we present evidence that the previously reported structural homology between sigma 1 and the adenovirus attachment protein, fiber, also extends to their respective receptors, which form similar dimeric structures. Because both receptors are located at regions of cell-cell contact, this similarity suggests that reovirus and adenovirus use conserved mechanisms of entry and pathways of infection.
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==About this Structure==
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nbq ConSurf].
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1NBQ is a [[Single protein]] structure of 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=1NBQ OCA].
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<div style="clear:both"></div>
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of human junctional adhesion molecule 1: implications for reovirus binding., Prota AE, Campbell JA, Schelling P, Forrest JC, Watson MJ, Peters TR, Aurrand-Lions M, Imhof BA, Dermody TS, Stehle T, Proc Natl Acad Sci U S A. 2003 Apr 29;100(9):5366-71. Epub 2003 Apr 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12697893 12697893]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Aurrand-Lions, M.]]
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[[Category: Aurrand-Lions M]]
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[[Category: Campbell, J A.]]
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[[Category: Campbell JA]]
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[[Category: Dermody, T S.]]
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[[Category: Dermody TS]]
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[[Category: Forrest, J C.]]
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[[Category: Forrest JC]]
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[[Category: Imhof, B A.]]
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[[Category: Imhof BA]]
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[[Category: Peters, T R.]]
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[[Category: Peters TR]]
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[[Category: Prota, A E.]]
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[[Category: Prota AE]]
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[[Category: Schelling, P.]]
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[[Category: Schelling P]]
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[[Category: Stehle, T.]]
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[[Category: Stehle T]]
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[[Category: Watson, M J.]]
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[[Category: Watson MJ]]
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[[Category: adhesion molecule]]
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[[Category: immunoglobulin superfamily]]
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[[Category: reovirus receptor]]
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[[Category: tight junction formation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:28:09 2008''
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Current revision

Crystal Structure of Human Junctional Adhesion Molecule Type 1

PDB ID 1nbq

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