1iqw: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1iqw.jpg|left|200px]]
- {{Structure
+==CRYSTAL STRUCTURE OF THE FAB FRAGMENT OF THE MOUSE ANTI-HUMAN FAS ANTIBODY HFE7A==
-|PDB= 1iqw |SIZE=350|CAPTION= <scene name='initialview01'>1iqw</scene>, resolution 2.50&Aring;
+<StructureSection load='1iqw' size='340' side='right'caption='[[1iqw]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND=
+<table><tr><td colspan='2'>[[1iqw]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1IQW FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
-|GENE=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1iqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iqw OCA], [https://pdbe.org/1iqw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iqw RCSB], [https://www.ebi.ac.uk/pdbsum/1iqw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iqw ProSAT]</span></td></tr>
-|DOMAIN=
+</table>
-|RELATEDENTRY=
+== Evolutionary Conservation ==
-|RESOURCES=<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.ebi.ac.uk/pdbsum/1iqw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1iqw RCSB]</span>
+[[Image:Consurf_key_small.gif|200px|right]]
-}}
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iq/1iqw_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1iqw ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Binding 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 FAB FRAGMENT OF THE MOUSE ANTI-HUMAN FAS ANTIBODY HFE7A'''
+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<ref>PMID:11754745</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1iqw" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-Binding 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.
+*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-IQW is a [[Protein complex]] structure of sequences 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].
+__TOC__
+</StructureSection>
-==Reference==
+[[Category: Large Structures]]
-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:[http://www.ncbi.nlm.nih.gov/pubmed/11754745 11754745]
 [[Category: Mus musculus]]
-[[Category: Protein complex]]
+[[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: anti_fa]]
-[[Category: apoptosis]]
-[[Category: fab]]
-[[Category: immunoglobulin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:23:25 2008''