2d39
From Proteopedia
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|PDB= 2d39 |SIZE=350|CAPTION= <scene name='initialview01'>2d39</scene>, resolution 1.9Å | |PDB= 2d39 |SIZE=350|CAPTION= <scene name='initialview01'>2d39</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d39 OCA], [http://www.ebi.ac.uk/pdbsum/2d39 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d39 RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Sugio, S.]] | [[Category: Sugio, S.]] | ||
[[Category: Tanio, M.]] | [[Category: Tanio, M.]] | ||
| - | [[Category: CA]] | ||
[[Category: ficolin]] | [[Category: ficolin]] | ||
[[Category: innate immunity system]] | [[Category: innate immunity system]] | ||
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[[Category: m-ficolin]] | [[Category: m-ficolin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:29:44 2008'' |
Revision as of 23:29, 30 March 2008
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| , resolution 1.9Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Trivalent Recognition Unit of Innate Immunity System; Crystal Structure of human M-ficolin Fibrinogen-like Domain
Overview
Ficolins are a kind of pathogen-recognition molecule in the innate immune systems. To investigate the discrimination mechanism between self and non-self by ficolins, we determined the crystal structure of the human M-ficolin fibrinogen-like domain (FD1), which is the ligand-binding domain, at 1.9A resolution. Although the FD1 monomer shares a common fold with the fibrinogen gamma fragment and tachylectin-5A, the Asp-282-Cys-283 peptide bond, which is the predicted ligand-binding site on the C-terminal P domain, is a normal trans bond, unlike the cases of the other two proteins. The trimeric formation of FD1 results in the separation of the three P domains, and the spatial arrangement of the three predicted ligand-binding sites on the trimer is very similar to that of the trimeric collectin, indicating that such an arrangement is generally required for pathogen-recognition. The ligand binding study of FD1 in solution indicated that the recombinant protein binds to N-acetyl-d-glucosamine and the peptide Gly-Pro-Arg-Pro and suggested that the ligand-binding region exhibits a conformational equilibrium involving cis-trans isomerization of the Asp-282-Cys-283 peptide bond. The crystal structure and the ligand binding study of FD1 provide an insight of the self- and non-self discrimination mechanism by ficolins.
About this Structure
2D39 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Trivalent recognition unit of innate immunity system: crystal structure of trimeric human M-ficolin fibrinogen-like domain., Tanio M, Kondo S, Sugio S, Kohno T, J Biol Chem. 2007 Feb 9;282(6):3889-95. Epub 2006 Dec 4. PMID:17148457
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