1gig
From Proteopedia
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| - | [[Image:1gig.gif|left|200px]] | ||
| - | + | ==REFINED THREE-DIMENSIONAL STRUCTURE OF THE FAB FRAGMENT OF A MURINE IGG1, LAMBDA ANTIBODY== | |
| - | + | <StructureSection load='1gig' size='340' side='right'caption='[[1gig]], [[Resolution|resolution]] 2.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1gig]] 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=1GIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GIG FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gig OCA], [https://pdbe.org/1gig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gig RCSB], [https://www.ebi.ac.uk/pdbsum/1gig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gig ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/Q99LC4_MOUSE Q99LC4_MOUSE] | |
| - | + | == Evolutionary Conservation == | |
| - | + | [[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/gi/1gig_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=1gig ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
We report the cDNA sequence determination and the crystal structure of the Fab fragment of a murine IgG1,lambda antibody (HC19), specific for an influenza virus hemagglutinin. The HC19 Fab-fragment structure has been refined; the crystallographic R-factor is 19.5% at 2.3 A resolution. We have compared the conformation of HC19 complementarity determining regions (CDRs) with those of CDR loops of Fab structures available from the Protein Data Bank. These loops were chosen based on the identity of key residues, following the canonical-structure approach; four CDRs have a main-chain conformation very similar to the canonical structure that had been identified. HC19 L1 CDR adopts a conformation clearly distinct from all L1 CDRs that belong to a chain of a different class or origin; this is determined by the nature of a few residues at positions in the sequence different from those of key residues in other light chains. This canonical structure should be representative of most murine lambda-class light chains, as inferred from the very high sequence homologies of these polypeptides. | We report the cDNA sequence determination and the crystal structure of the Fab fragment of a murine IgG1,lambda antibody (HC19), specific for an influenza virus hemagglutinin. The HC19 Fab-fragment structure has been refined; the crystallographic R-factor is 19.5% at 2.3 A resolution. We have compared the conformation of HC19 complementarity determining regions (CDRs) with those of CDR loops of Fab structures available from the Protein Data Bank. These loops were chosen based on the identity of key residues, following the canonical-structure approach; four CDRs have a main-chain conformation very similar to the canonical structure that had been identified. HC19 L1 CDR adopts a conformation clearly distinct from all L1 CDRs that belong to a chain of a different class or origin; this is determined by the nature of a few residues at positions in the sequence different from those of key residues in other light chains. This canonical structure should be representative of most murine lambda-class light chains, as inferred from the very high sequence homologies of these polypeptides. | ||
| - | + | Refined three-dimensional structure of the Fab fragment of a murine IgGl,lambda antibody.,Bizebard T, Daniels R, Kahn R, Golinelli-Pimpaneau B, Skehel JJ, Knossow M Acta Crystallogr D Biol Crystallogr. 1994 Sep 1;50(Pt 5):768-77. PMID:15299376<ref>PMID:15299376</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1gig" style="background-color:#fffaf0;"></div> | |
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| - | + | ||
| - | + | ==See Also== | |
| + | *[[Antibody 3D structures|Antibody 3D structures]] | ||
| + | *[[Sandbox 20009|Sandbox 20009]] | ||
| + | *[[3D structures of non-human antibody|3D structures of non-human antibody]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Bizebard T]] | ||
| + | [[Category: Knossow M]] | ||
Current revision
REFINED THREE-DIMENSIONAL STRUCTURE OF THE FAB FRAGMENT OF A MURINE IGG1, LAMBDA ANTIBODY
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