2os5

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[[Image:2os5.jpg|left|200px]]<br /><applet load="2os5" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2os5.jpg|left|200px]]
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caption="2os5, resolution 1.60&Aring;" />
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'''Macrophage migration inhibitory factor from Ancylostoma ceylanicum'''<br />
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{{Structure
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|PDB= 2os5 |SIZE=350|CAPTION= <scene name='initialview01'>2os5</scene>, resolution 1.60&Aring;
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|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Residue+D+201'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Residue+A+202'>AC2</scene>, <scene name='pdbsite=AC3:So4+Binding+Site+For+Residue+A+203'>AC3</scene> and <scene name='pdbsite=AC4:So4+Binding+Site+For+Residue+B+204'>AC4</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''Macrophage migration inhibitory factor from Ancylostoma ceylanicum'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2OS5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Ancylostoma_ceylanicum Ancylostoma ceylanicum] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=AC1:So4+Binding+Site+For+Residue+D+201'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Residue+A+202'>AC2</scene>, <scene name='pdbsite=AC3:So4+Binding+Site+For+Residue+A+203'>AC3</scene> and <scene name='pdbsite=AC4:So4+Binding+Site+For+Residue+B+204'>AC4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OS5 OCA].
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2OS5 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Ancylostoma_ceylanicum Ancylostoma ceylanicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OS5 OCA].
==Reference==
==Reference==
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Structural and functional characterization of a secreted hookworm Macrophage Migration Inhibitory Factor (MIF) that interacts with the human MIF receptor CD74., Cho Y, Jones BF, Vermeire JJ, Leng L, DiFedele L, Harrison LM, Xiong H, Kwong YK, Chen Y, Bucala R, Lolis E, Cappello M, J Biol Chem. 2007 Aug 10;282(32):23447-56. Epub 2007 Jun 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17567581 17567581]
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Structural and functional characterization of a secreted hookworm Macrophage Migration Inhibitory Factor (MIF) that interacts with the human MIF receptor CD74., Cho Y, Jones BF, Vermeire JJ, Leng L, DiFedele L, Harrison LM, Xiong H, Kwong YK, Chen Y, Bucala R, Lolis E, Cappello M, J Biol Chem. 2007 Aug 10;282(32):23447-56. Epub 2007 Jun 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17567581 17567581]
[[Category: Ancylostoma ceylanicum]]
[[Category: Ancylostoma ceylanicum]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: nematode]]
[[Category: nematode]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:21:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:03:49 2008''

Revision as of 16:03, 20 March 2008

Image:2os5.jpg


PDB ID 2os5

Drag the structure with the mouse to rotate
, resolution 1.60Å
Sites: , , and
Ligands:
Coordinates: save as pdb, mmCIF, xml



Macrophage migration inhibitory factor from Ancylostoma ceylanicum


Overview

Hookworms, parasitic nematodes that infect nearly one billion people worldwide, are a major cause of anemia and malnutrition. We hypothesize that hookworms actively manipulate the host immune response through the production of specific molecules designed to facilitate infection by larval stages and adult worm survival within the intestine. A full-length cDNA encoding a secreted orthologue of the human cytokine, Macrophage Migration Inhibitory Factor (MIF) has been cloned from the hookworm Ancylostoma ceylanicum. Elucidation of the three-dimensional crystal structure of recombinant AceMIF (rAceMIF) revealed an overall structural homology with significant differences in the tautomerase sites of the human and hookworm proteins. The relative bioactivities of human and hookworm MIF proteins were compared using in vitro assays of tautomerase activity, macrophage migration, and binding to MIF receptor CD74. The activity of rAceMIF was not inhibited by the ligand ISO-1, which was previously determined to be an inhibitor of the catalytic site of human MIF. These data define unique immunological, structural, and functional characteristics of AceMIF, thereby establishing the potential for selectively inhibiting the hookworm cytokine as a means of reducing parasite survival and disease pathogenesis.

About this Structure

2OS5 is a Protein complex structure of sequences from Ancylostoma ceylanicum. Full crystallographic information is available from OCA.

Reference

Structural and functional characterization of a secreted hookworm Macrophage Migration Inhibitory Factor (MIF) that interacts with the human MIF receptor CD74., Cho Y, Jones BF, Vermeire JJ, Leng L, DiFedele L, Harrison LM, Xiong H, Kwong YK, Chen Y, Bucala R, Lolis E, Cappello M, J Biol Chem. 2007 Aug 10;282(32):23447-56. Epub 2007 Jun 13. PMID:17567581

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