2aty: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2aty]] is a 2 chain structure with sequence 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=2ATY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ATY FirstGlance]. <br> | <table><tr><td colspan='2'>[[2aty]] is a 2 chain structure with sequence 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=2ATY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ATY FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1igy|1igy]], [[1ghq|1ghq]], [[1w2r|1w2r]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1igy|1igy]], [[1ghq|1ghq]], [[1w2r|1w2r]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2aty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aty OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2aty RCSB], [http://www.ebi.ac.uk/pdbsum/2aty PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2aty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aty OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2aty RCSB], [http://www.ebi.ac.uk/pdbsum/2aty PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Aslam, M | [[Category: Aslam, M]] | ||
[[Category: Gilbert, H E | [[Category: Gilbert, H E]] | ||
[[Category: Guthridge, J M | [[Category: Guthridge, J M]] | ||
[[Category: Holers, V M | [[Category: Holers, V M]] | ||
[[Category: Perkins, S J | [[Category: Perkins, S J]] | ||
[[Category: Antibody]] | [[Category: Antibody]] | ||
[[Category: Complement]] | [[Category: Complement]] | ||
[[Category: Immune system]] | [[Category: Immune system]] | ||
[[Category: Immunoglobulin fold]] | [[Category: Immunoglobulin fold]] | ||
Revision as of 12:36, 8 January 2015
Complement receptor chimaeric conjugate CR2-IgComplement receptor chimaeric conjugate CR2-Ig
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedComplement receptor 2 (CR2; CD21) is a membrane-bound regulator of complement activation, being comprised of 15 or 16 short complement repeat (SCR) domains. A recombinant glycosylated human CR2 SCR 1-2 domain pair was engineered with the Fc fragment of a mouse IgG1 antibody to create a chimaera CR2-Ig containing the major ligand binding domains. Such a chimaera has therapeutic potential as a complement inhibitor or immune modulator. X-ray and neutron scattering and analytical ultracentrifugation identified its domain structure in solution, and provided a comparison with controversial folded-back crystal structures for deglycosylated CR2 SCR 1-2. The radius of gyration R(G) of CR2-Ig was determined to be 5.39(+/-0.14) nm and 5.29(+/-0.01) nm by X-ray and neutron scattering, respectively. The maximum dimension of CR2-Ig was determined to be 17 nm. The molecular mass of CR2-Ig ranged between 101,000 Da and 107,000 Da as determined by neutron scattering and sedimentation equilibrium, in good agreement with the sequence-derived value of 106,600 Da. Sedimentation velocity gave a sedimentation coefficient of 4.49(+/-0.11) S. Stereochemically complete models for CR2-Ig were constructed from crystal structures for the CR2 SCR 1-2 and mouse IgG1 Fc fragments. The two SCR domains and the Fc fragment were joined by randomised conformational peptides. The analysis of 35,000 possible CR2-Ig models showed that only those models in which the two SCR domains were arranged in an open V-shape in random orientations about the Fc fragment accounted for the scattering and sedimentation data. It was not possible to define one single conformational family of Fab-like fragment relative to the Fc fragment. This flexibility is attributed to the relatively long linker sequence and the absence of the antibody light chain from CR2-Ig. The modelling also confirmed that the structure of CR2 SCR 1-2 is more extended in solution than in its crystal structure. Extended flexible linker structures in the complement chimaeric conjugate CR2-Ig by scattering, analytical ultracentrifugation and constrained modelling: implications for function and therapy.,Gilbert HE, Aslam M, Guthridge JM, Holers VM, Perkins SJ J Mol Biol. 2006 Feb 17;356(2):397-412. Epub 2005 Dec 5. PMID:16375923[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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