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1frg

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(New page: 200px<br /> <applet load="1frg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1frg, resolution 2.8&Aring;" /> '''CRYSTAL STRUCTURE, S...)
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[[Image:1frg.gif|left|200px]]<br />
 
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<applet load="1frg" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1frg, resolution 2.8&Aring;" />
 
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'''CRYSTAL STRUCTURE, SEQUENCE, AND EPITOPE MAPPING OF A PEPTIDE COMPLEX OF AN ANTI-INFLUENZA HA PEPTIDE ANTIBODY FAB 26(SLASH)9: FINE-TUNING ANTIBODY SPECIFICITY'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE, SEQUENCE, AND EPITOPE MAPPING OF A PEPTIDE COMPLEX OF AN ANTI-INFLUENZA HA PEPTIDE ANTIBODY FAB 26(SLASH)9: FINE-TUNING ANTIBODY SPECIFICITY==
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The three-dimensional structure of the complex of a second anti-peptide, antibody (Fab 26/9) that recognizes the same six-residue epitope of an, immunogenic peptide from influenza virus hemagglutinin (HA1; 75-110) as, Fab 17/9 with the peptide has been determined at 2.8 A resolution. The, amino acid sequence of the variable region of the 26/9 antibody differs in, 24 positions from that of 17/9, the first antibody in this series for, which several ligand-bound and free structures have been determined and, refined. Comparison of the 26/9-peptide with the 17/9-peptide complex, structures shows that the two Fabs are very similar (r.m.s.d. 0.5 to 0.8, A) and that the peptide antigen (101-107) has virtually the same, conformation (r.m.s.d. 0.3 to 0.8 A) when bound to both antibodies. A, sequence difference in the 26/9 binding pocket (L94; His in 26/9, Asn in, 17/9) results in an interaction with a bound water molecule that is not, seen in the 17/9 structures. Epitope mapping shows that the relative, specificity of 26/9 and 17/9 antibodies for individual positions of the, peptide antigen are slightly different. Amino acid substitutions in the, peptide, particularly at position SerP107, are tolerated to different, extents by 17/9 and 26/9. Structural and sequence analysis suggests that, amino acid differences near the peptide-binding site are responsible for, altering slightly the specificity of 26/9 for three peptide residues and, illustrates how amino acid substitutions can modify antibody-antigen, interactions and thereby modulate antibody specificity.
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<StructureSection load='1frg' size='340' side='right'caption='[[1frg]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1frg]] is a 3 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=1FRG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FRG FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1frg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1frg OCA], [https://pdbe.org/1frg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1frg RCSB], [https://www.ebi.ac.uk/pdbsum/1frg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1frg ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/IGKC_MOUSE IGKC_MOUSE]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fr/1frg_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1frg ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1FRG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with ACE and NH2 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FRG OCA].
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*[[Antibody 3D structures|Antibody 3D structures]]
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*[[3D structures of non-human antibody|3D structures of non-human antibody]]
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==Reference==
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__TOC__
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Crystal structure of a peptide complex of anti-influenza peptide antibody Fab 26/9. Comparison of two different antibodies bound to the same peptide antigen., Churchill ME, Stura EA, Pinilla C, Appel JR, Houghten RA, Kono DH, Balderas RS, Fieser GG, Schulze-Gahmen U, Wilson IA, J Mol Biol. 1994 Aug 26;241(4):534-56. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7520084 7520084]
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</StructureSection>
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Churchill, M.E.A.]]
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[[Category: Mus musculus]]
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[[Category: Wilson, I.A.]]
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[[Category: Churchill MEA]]
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[[Category: ACE]]
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[[Category: Wilson IA]]
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[[Category: NH2]]
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[[Category: immunoglobulin/virus hemagglutinin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:30:37 2007''
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Current revision

CRYSTAL STRUCTURE, SEQUENCE, AND EPITOPE MAPPING OF A PEPTIDE COMPLEX OF AN ANTI-INFLUENZA HA PEPTIDE ANTIBODY FAB 26(SLASH)9: FINE-TUNING ANTIBODY SPECIFICITY

PDB ID 1frg

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