1c3d

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(New page: 200px<br /> <applet load="1c3d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c3d, resolution 1.80&Aring;" /> '''X-RAY CRYSTAL STRUC...)
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[[Image:1c3d.gif|left|200px]]<br /><applet load="1c3d" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1c3d" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1c3d, resolution 1.80&Aring;" />
caption="1c3d, resolution 1.80&Aring;" />
'''X-RAY CRYSTAL STRUCTURE OF C3D: A C3 FRAGMENT AND LIGAND FOR COMPLEMENT RECEPTOR 2'''<br />
'''X-RAY CRYSTAL STRUCTURE OF C3D: A C3 FRAGMENT AND LIGAND FOR COMPLEMENT RECEPTOR 2'''<br />
==Overview==
==Overview==
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Activation and covalent attachment of complement component C3 to pathogens, is the key step in complement-mediated host defense. Additionally, the, antigen-bound C3d fragment interacts with complement receptor 2 (CR2; also, known as CD21) on B cells and thereby contributes to the initiation of an, acquired humoral response. The x-ray crystal structure of human C3d solved, at 2.0 angstroms resolution reveals an alpha-alpha barrel with the, residues responsible for thioester formation and covalent attachment at, one end and an acidic pocket at the other. The structure supports a model, whereby the transition of native C3 to its functionally active state, involves the disruption of a complementary domain interface and provides, insight into the basis for the interaction between C3d and CR2.
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Activation and covalent attachment of complement component C3 to pathogens is the key step in complement-mediated host defense. Additionally, the antigen-bound C3d fragment interacts with complement receptor 2 (CR2; also known as CD21) on B cells and thereby contributes to the initiation of an acquired humoral response. The x-ray crystal structure of human C3d solved at 2.0 angstroms resolution reveals an alpha-alpha barrel with the residues responsible for thioester formation and covalent attachment at one end and an acidic pocket at the other. The structure supports a model whereby the transition of native C3 to its functionally active state involves the disruption of a complementary domain interface and provides insight into the basis for the interaction between C3d and CR2.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1C3D 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 GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C3D OCA].
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1C3D 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=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C3D OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Diefenbach, R.J.]]
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[[Category: Diefenbach, R J.]]
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[[Category: Isenman, D.E.]]
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[[Category: Isenman, D E.]]
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[[Category: Jones, R.G.]]
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[[Category: Jones, R G.]]
[[Category: Nagar, B.]]
[[Category: Nagar, B.]]
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[[Category: Rini, J.M.]]
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[[Category: Rini, J M.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: alpha-alpha barrel]]
[[Category: alpha-alpha barrel]]
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[[Category: complement]]
[[Category: complement]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:16:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:01:59 2008''

Revision as of 10:01, 21 February 2008


1c3d, resolution 1.80Å

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X-RAY CRYSTAL STRUCTURE OF C3D: A C3 FRAGMENT AND LIGAND FOR COMPLEMENT RECEPTOR 2

Contents

Overview

Activation and covalent attachment of complement component C3 to pathogens is the key step in complement-mediated host defense. Additionally, the antigen-bound C3d fragment interacts with complement receptor 2 (CR2; also known as CD21) on B cells and thereby contributes to the initiation of an acquired humoral response. The x-ray crystal structure of human C3d solved at 2.0 angstroms resolution reveals an alpha-alpha barrel with the residues responsible for thioester formation and covalent attachment at one end and an acidic pocket at the other. The structure supports a model whereby the transition of native C3 to its functionally active state involves the disruption of a complementary domain interface and provides insight into the basis for the interaction between C3d and CR2.

Disease

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

About this Structure

1C3D is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

X-ray crystal structure of C3d: a C3 fragment and ligand for complement receptor 2., Nagar B, Jones RG, Diefenbach RJ, Isenman DE, Rini JM, Science. 1998 May 22;280(5367):1277-81. PMID:9596584

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