1iqw: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1iqw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IQW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IQW FirstGlance]. <br> | <table><tr><td colspan='2'>[[1iqw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IQW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IQW FirstGlance]. <br> | ||
</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=1iqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iqw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1iqw RCSB], [http://www.ebi.ac.uk/pdbsum/1iqw PDBsum]</span></td></tr> | </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=1iqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iqw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1iqw RCSB], [http://www.ebi.ac.uk/pdbsum/1iqw 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: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Hanzawa, H | [[Category: Hanzawa, H]] | ||
[[Category: Haruyama, H]] | [[Category: Haruyama, H]] | ||
[[Category: Hata, T | [[Category: Hata, T]] | ||
[[Category: Ichikawa, K | [[Category: Ichikawa, K]] | ||
[[Category: Ito, S | [[Category: Ito, S]] | ||
[[Category: Ohsumi, J | [[Category: Ohsumi, J]] | ||
[[Category: Serizawa, N | [[Category: Serizawa, N]] | ||
[[Category: Takayama, T | [[Category: Takayama, T]] | ||
[[Category: Agonistic antibody]] | [[Category: Agonistic antibody]] | ||
[[Category: Anti_fa]] | [[Category: Anti_fa]] | ||
Revision as of 12:49, 2 January 2015
CRYSTAL STRUCTURE OF THE FAB FRAGMENT OF THE MOUSE ANTI-HUMAN FAS ANTIBODY HFE7ACRYSTAL STRUCTURE OF THE FAB FRAGMENT OF THE MOUSE ANTI-HUMAN FAS ANTIBODY HFE7A
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 PubMedBinding of Fas ligand to Fas induces apoptosis. The Fas-Fas ligand system plays important roles in many biological processes, including the elimination of autoreactive lymphoid cells. The mouse anti-human Fas monoclonal antibody HFE7A (m-HFE7A), which induces apoptosis, has been humanized based on a structure predicted by homology modeling. A version of humanized HFE7A is currently under development for the treatment of autoimmune diseases such as rheumatoid arthritis. For a deeper understanding of the protein engineering aspect of antibody humanization, for which information on the three-dimensional structure is essential, we determined the crystal structure of the m-HFE7A antigen-binding fragment (Fab) by X-ray crystallography at 2.5 A resolution. The main-chain conformation of the five loops in the six complementarity-determining regions (CDRs) was correctly predicted with root-mean-square deviations of 0.30-1.04 A based on a comparison of the crystal structure with the predicted structure. The CDR-H3 conformation of the crystal structure, which was not classified as one of the canonical structures, was completely different from that of the predicted structure but adopted the conformation which followed the "H3-rules." The results of charge distribution analysis of the antigen-binding site suggest that electrostatic interactions may be important for its binding to Fas. Crystal structure of the antigen-binding fragment of apoptosis-inducing mouse anti-human Fas monoclonal antibody HFE7A.,Ito S, Takayama T, Hanzawa H, Ichikawa K, Ohsumi J, Serizawa N, Hata T, Haruyama H J Biochem. 2002 Jan;131(1):137-43. PMID:11754745[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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