1c3d: Difference between revisions

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New page: left|200px<br /> <applet load="1c3d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c3d, resolution 1.80Å" /> '''X-RAY CRYSTAL STRUC...
 
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[[Image:1c3d.gif|left|200px]]<br />
[[Image:1c3d.gif|left|200px]]<br /><applet load="1c3d" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1c3d" size="450" color="white" frame="true" align="right" spinBox="true"  
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==
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.
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==
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].  
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]]
[[Category: Diefenbach, R.J.]]
[[Category: Diefenbach, R J.]]
[[Category: Isenman, D.E.]]
[[Category: Isenman, D E.]]
[[Category: Jones, R.G.]]
[[Category: Jones, R G.]]
[[Category: Nagar, B.]]
[[Category: Nagar, B.]]
[[Category: Rini, J.M.]]
[[Category: Rini, J M.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: alpha-alpha barrel]]
[[Category: alpha-alpha barrel]]
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[[Category: complement]]
[[Category: complement]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:16:57 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:01:59 2008''

Revision as of 13:01, 21 February 2008

File:1c3d.gif


1c3d, resolution 1.80Å

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

OverviewOverview

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.

DiseaseDisease

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

About this StructureAbout this Structure

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

ReferenceReference

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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