2d39: Difference between revisions

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[[Image:2d39.gif|left|200px]]<br />

[[Image:2d39.gif|left|200px]]<br /><applet load="2d39" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="2d39" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="2d39, resolution 1.9Å" />

'''Trivalent Recognition Unit of Innate Immunity System; Crystal Structure of human M-ficolin Fibrinogen-like Domain'''<br />

==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.

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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2D39 OCA].

2D39 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D39 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17148457 17148457]

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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17148457 17148457]

[[Category: Homo sapiens]]

[[Category: Single protein]]

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[[Category: m-ficolin]]

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-[[Image:2d39.gif|left|200px]]<br />
+[[Image:2d39.gif|left|200px]]<br /><applet load="2d39" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="2d39" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="2d39, resolution 1.9&Aring;" />
 '''Trivalent Recognition Unit of Innate Immunity System; Crystal Structure of human M-ficolin Fibrinogen-like Domain'''<br />
 ==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.
+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==
-D39 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2D39 OCA].
+D39 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D39 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17148457 17148457]
+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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17148457 17148457]
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
@@ Line 24: / Line 23: @@
 [[Category: m-ficolin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:25:48 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:56 2008''