2icf

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[[Image:2icf.gif|left|200px]]<br /><applet load="2icf" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2icf.gif|left|200px]]
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caption="2icf, resolution 4.10&Aring;" />
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'''CRIg bound to C3b'''<br />
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{{Structure
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|PDB= 2icf |SIZE=350|CAPTION= <scene name='initialview01'>2icf</scene>, resolution 4.10&Aring;
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|SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Residue+A+643'>AC1</scene>, <scene name='pdbsite=AC2:Nag+Binding+Site+For+Residue+A+644'>AC2</scene>, <scene name='pdbsite=AC3:Bma+Binding+Site+For+Residue+A+645'>AC3</scene>, <scene name='pdbsite=AC4:Nag+Binding+Site+For+Residue+B+5'>AC4</scene> and <scene name='pdbsite=AC5:Ca+Binding+Site+For+Residue+A+647'>AC5</scene>
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''CRIg bound to C3b'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2ICF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Nag+Binding+Site+For+Residue+A+643'>AC1</scene>, <scene name='pdbsite=AC2:Nag+Binding+Site+For+Residue+A+644'>AC2</scene>, <scene name='pdbsite=AC3:Bma+Binding+Site+For+Residue+A+645'>AC3</scene>, <scene name='pdbsite=AC4:Nag+Binding+Site+For+Residue+B+5'>AC4</scene> and <scene name='pdbsite=AC5:Ca+Binding+Site+For+Residue+A+647'>AC5</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ICF OCA].
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2ICF is a [[Protein complex]] structure of sequences 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=2ICF OCA].
==Reference==
==Reference==
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Structure of C3b in complex with CRIg gives insights into regulation of complement activation., Wiesmann C, Katschke KJ, Yin J, Helmy KY, Steffek M, Fairbrother WJ, McCallum SA, Embuscado L, DeForge L, Hass PE, van Lookeren Campagne M, Nature. 2006 Nov 9;444(7116):217-20. Epub 2006 Oct 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17051150 17051150]
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Structure of C3b in complex with CRIg gives insights into regulation of complement activation., Wiesmann C, Katschke KJ, Yin J, Helmy KY, Steffek M, Fairbrother WJ, McCallum SA, Embuscado L, DeForge L, Hass PE, van Lookeren Campagne M, Nature. 2006 Nov 9;444(7116):217-20. Epub 2006 Oct 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17051150 17051150]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: immune system]]
[[Category: immune system]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:51:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:27:51 2008''

Revision as of 15:27, 20 March 2008

Image:2icf.gif


PDB ID 2icf

Drag the structure with the mouse to rotate
, resolution 4.10Å
Sites: , , , and
Ligands: and
Coordinates: save as pdb, mmCIF, xml



CRIg bound to C3b


Contents

Overview

The complement system is a key part of the innate immune system, and is required for clearance of pathogens from the bloodstream. After exposure to pathogens, the third component of the complement system, C3, is cleaved to C3b which, after recruitment of factor B, initiates formation of the alternative pathway convertases. CRIg, a complement receptor expressed on macrophages, binds to C3b and iC3b mediating phagocytosis of the particles, but it is unknown how CRIg selectively recognizes proteolytic C3-fragments and whether binding of CRIg to C3b inhibits convertase activation. Here we present the crystal structure of C3b in complex with CRIg and, using CRIg mutants, provide evidence that CRIg acts as an inhibitor of the alternative pathway of complement. The structure shows that activation of C3 induces major structural rearrangements, including a dramatic movement (>80 A) of the thioester-bond-containing domain through which C3b attaches to pathogen surfaces. We show that CRIg is not only a phagocytic receptor, but also a potent inhibitor of the alternative pathway convertases. The structure provides insights into the complex macromolecular structural rearrangements that occur during complement activation and inhibition. Moreover, our structure-function studies relating the structural basis of complement activation and the means by which CRIg inhibits the convertases provide important clues to the development of therapeutics that target complement.

Disease

Known diseases associated with this structure: C3 deficiency OMIM:[120700], Macular degeneration, age-related, 9 OMIM:[120700]

About this Structure

2ICF is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of C3b in complex with CRIg gives insights into regulation of complement activation., Wiesmann C, Katschke KJ, Yin J, Helmy KY, Steffek M, Fairbrother WJ, McCallum SA, Embuscado L, DeForge L, Hass PE, van Lookeren Campagne M, Nature. 2006 Nov 9;444(7116):217-20. Epub 2006 Oct 15. PMID:17051150

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