1ckl
From Proteopedia
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| - | [[Image:1ckl.gif|left|200px]] | + | [[Image:1ckl.gif|left|200px]] |
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| - | '''N-TERMINAL TWO DOMAINS OF HUMAN CD46 (MEMBRANE COFACTOR PROTEIN, MCP)''' | + | {{Structure |
| + | |PDB= 1ckl |SIZE=350|CAPTION= <scene name='initialview01'>1ckl</scene>, resolution 3.100Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''N-TERMINAL TWO DOMAINS OF HUMAN CD46 (MEMBRANE COFACTOR PROTEIN, MCP)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CKL is a [ | + | 1CKL 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=1CKL OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10357804 10357804] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: virus receptor]] | [[Category: virus receptor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:25:32 2008'' |
Revision as of 08:25, 20 March 2008
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| , resolution 3.100Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
N-TERMINAL TWO DOMAINS OF HUMAN CD46 (MEMBRANE COFACTOR PROTEIN, MCP)
Contents |
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.
Disease
Known diseases associated with this structure: Hemolytic-uremic syndrome OMIM:[120920], Measles, susceptibility to OMIM:[120920]
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 Thu Mar 20 10:25:32 2008
