1ckl: Difference between revisions

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[[Image:1ckl.gif|left|200px]]
[[Image:1ckl.gif|left|200px]]


{{Structure
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|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ckl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ckl OCA], [http://www.ebi.ac.uk/pdbsum/1ckl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ckl RCSB]</span>
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'''N-TERMINAL TWO DOMAINS OF HUMAN CD46 (MEMBRANE COFACTOR PROTEIN, MCP)'''
'''N-TERMINAL TWO DOMAINS OF HUMAN CD46 (MEMBRANE COFACTOR PROTEIN, MCP)'''
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[[Category: Larvie, M.]]
[[Category: Larvie, M.]]
[[Category: Stehle, T.]]
[[Category: Stehle, T.]]
[[Category: complement cofactor]]
[[Category: Complement cofactor]]
[[Category: glycoprotein]]
[[Category: Glycoprotein]]
[[Category: measles virus]]
[[Category: Measles virus]]
[[Category: scr]]
[[Category: Scr]]
[[Category: short consensus repeat]]
[[Category: Short consensus repeat]]
[[Category: virus receptor]]
[[Category: Virus receptor]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:23:33 2008''

Revision as of 09:50, 2 May 2008

File:1ckl.gif

Template:STRUCTURE 1ckl

N-TERMINAL TWO DOMAINS OF HUMAN CD46 (MEMBRANE COFACTOR PROTEIN, MCP)


Overview

Measles virus is a paramyxovirus which, like other members of the family such as respiratory syncytial virus, is a major cause of morbidity and mortality worldwide. The cell surface receptor for measles virus in humans is CD46, a complement cofactor. We report here the crystal structure at 3.1 A resolution of the measles virus-binding fragment of CD46. The structure reveals the architecture and spatial arrangement of two glycosylated short consensus repeats with a pronounced interdomain bend and some flexibility at the domain interface. Amino acids involved in measles virus binding define a large, glycan-free surface that extends from the top of the first to the bottom of the second repeat. The extended virus-binding surface of CD46 differs strikingly from those reported for the human virus receptor proteins CD4 and intercellular cell adhesion molecule-1 (ICAM-1), suggesting that the CD46 structure utilizes a novel mode of virus recognition. A highly hydrophobic and protruding loop at the base of the first repeat bears a critical virus-binding residue, thereby defining an important recognition epitope. Molecules that mimic the conformation of this loop potentially could be effective anti-viral agents by preventing binding of measles virus to CD46.

About this Structure

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

Reference

Crystal structure of two CD46 domains reveals an extended measles virus-binding surface., Casasnovas JM, Larvie M, Stehle T, EMBO J. 1999 Jun 1;18(11):2911-22. PMID:10357804 Page seeded by OCA on Fri May 2 12:50:00 2008

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