1hi6

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(New page: 200px<br /> <applet load="1hi6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hi6, resolution 2.55&Aring;" /> '''ANTI-P24 (HIV-1) FA...)
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[[Image:1hi6.gif|left|200px]]<br />
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[[Image:1hi6.gif|left|200px]]<br /><applet load="1hi6" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1hi6" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1hi6, resolution 2.55&Aring;" />
caption="1hi6, resolution 2.55&Aring;" />
'''ANTI-P24 (HIV-1) FAB FRAGMENT CB41 COMPLEXED WITH A PEPTIDE'''<br />
'''ANTI-P24 (HIV-1) FAB FRAGMENT CB41 COMPLEXED WITH A PEPTIDE'''<br />
==Overview==
==Overview==
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The X-ray crystal structures of an anti-p24 (HIV-1) monoclonal antibody, Fab fragment alone and in complexes with the epitope peptide GATPQDLNTnL, (n = norleucine), an epitope-homologous peptide GATPEDLNQKLAGN, as well as, two unrelated peptides GLYEWGGARITNTD and efslkGpllqwrsG (D-peptide), are, presented to a maximum resolution of 2.6 A. The latter three peptides were, identified from screening synthetic combinatorial peptide libraries., Although all peptides bind to the same antigen combining site, the, nonhomologous peptides adopt different binding conformations and also form, their critical contacts with different antibody residues. Only small, readjustments are observed within the framework of the Fab fragment upon, binding.
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The X-ray crystal structures of an anti-p24 (HIV-1) monoclonal antibody Fab fragment alone and in complexes with the epitope peptide GATPQDLNTnL (n = norleucine), an epitope-homologous peptide GATPEDLNQKLAGN, as well as two unrelated peptides GLYEWGGARITNTD and efslkGpllqwrsG (D-peptide), are presented to a maximum resolution of 2.6 A. The latter three peptides were identified from screening synthetic combinatorial peptide libraries. Although all peptides bind to the same antigen combining site, the nonhomologous peptides adopt different binding conformations and also form their critical contacts with different antibody residues. Only small readjustments are observed within the framework of the Fab fragment upon binding.
==About this Structure==
==About this Structure==
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1HI6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HI6 OCA].
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1HI6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HI6 OCA].
==Reference==
==Reference==
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[[Category: polyspecificity]]
[[Category: polyspecificity]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 14:05:43 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:01:29 2008''

Revision as of 11:01, 21 February 2008


1hi6, resolution 2.55Å

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ANTI-P24 (HIV-1) FAB FRAGMENT CB41 COMPLEXED WITH A PEPTIDE

Overview

The X-ray crystal structures of an anti-p24 (HIV-1) monoclonal antibody Fab fragment alone and in complexes with the epitope peptide GATPQDLNTnL (n = norleucine), an epitope-homologous peptide GATPEDLNQKLAGN, as well as two unrelated peptides GLYEWGGARITNTD and efslkGpllqwrsG (D-peptide), are presented to a maximum resolution of 2.6 A. The latter three peptides were identified from screening synthetic combinatorial peptide libraries. Although all peptides bind to the same antigen combining site, the nonhomologous peptides adopt different binding conformations and also form their critical contacts with different antibody residues. Only small readjustments are observed within the framework of the Fab fragment upon binding.

About this Structure

1HI6 is a Protein complex structure of sequences from Mus musculus with as ligand. Full crystallographic information is available from OCA.

Reference

Crystallographic analysis of anti-p24 (HIV-1) monoclonal antibody cross-reactivity and polyspecificity., Keitel T, Kramer A, Wessner H, Scholz C, Schneider-Mergener J, Hohne W, Cell. 1997 Dec 12;91(6):811-20. PMID:9413990

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