1nbq

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[[Image:1nbq.jpg|left|200px]]
[[Image:1nbq.jpg|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1nbq", creates the "Structure Box" on the page.
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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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{{STRUCTURE_1nbq| PDB=1nbq | SCENE= }}
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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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'''Crystal Structure of Human Junctional Adhesion Molecule Type 1'''
'''Crystal Structure of Human Junctional Adhesion Molecule Type 1'''
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[[Category: Stehle, T.]]
[[Category: Stehle, T.]]
[[Category: Watson, M J.]]
[[Category: Watson, M J.]]
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[[Category: adhesion molecule]]
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[[Category: Adhesion molecule]]
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[[Category: immunoglobulin superfamily]]
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[[Category: Immunoglobulin superfamily]]
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[[Category: reovirus receptor]]
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[[Category: Reovirus receptor]]
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[[Category: tight junction formation]]
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[[Category: Tight junction formation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:20:30 2008''
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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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Revision as of 23:20, 2 May 2008

Template:STRUCTURE 1nbq

Crystal Structure of Human Junctional Adhesion Molecule Type 1


Overview

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.

About this Structure

1NBQ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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:12697893 Page seeded by OCA on Sat May 3 02:20:30 2008

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