1frg: Difference between revisions

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[[Image:1frg.gif|left|200px]]<br /><applet load="1frg" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1frg.gif|left|200px]]
caption="1frg, resolution 2.8&Aring;" />
 
'''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 />
{{Structure
|PDB= 1frg |SIZE=350|CAPTION= <scene name='initialview01'>1frg</scene>, resolution 2.8&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> and <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene>
|ACTIVITY=
|GENE=
}}
 
'''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'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1FRG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FRG OCA].  
1FRG is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FRG OCA].  


==Reference==
==Reference==
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]
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://www.ncbi.nlm.nih.gov/pubmed/7520084 7520084]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Churchill, M E.A.]]
[[Category: Churchill, M E.A.]]
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[[Category: immunoglobulin/virus hemagglutinin]]
[[Category: immunoglobulin/virus hemagglutinin]]


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Revision as of 12:13, 20 March 2008

File:1frg.gif


PDB ID 1frg

Drag the structure with the mouse to rotate
, resolution 2.8Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



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


OverviewOverview

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.

About this StructureAbout this Structure

1FRG is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

ReferenceReference

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:7520084

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