1hh9
From Proteopedia
(New page: 200px<br /> <applet load="1hh9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hh9, resolution 2.7Å" /> '''ANTI-P24 (HIV-1) FAB...) |
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| - | [[Image:1hh9. | + | [[Image:1hh9.jpg|left|200px]]<br /><applet load="1hh9" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1hh9" size=" | + | |
caption="1hh9, resolution 2.7Å" /> | caption="1hh9, resolution 2.7Å" /> | ||
'''ANTI-P24 (HIV-1) FAB FRAGMENT CB41 COMPLEXED WITH A PEPTIDE'''<br /> | '''ANTI-P24 (HIV-1) FAB FRAGMENT CB41 COMPLEXED WITH A PEPTIDE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HH9 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:// | + | 1HH9 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=1HH9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: polyspecificity]] | [[Category: polyspecificity]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:56:45 2008'' |
Revision as of 13:56, 15 February 2008
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ANTI-P24 (HIV-1) FAB FRAGMENT CB41 COMPLEXED WITH A PEPTIDE
Overview
We identified evolutionary pathways for the inter- conversion of three, sequentially and structurally unrelated peptides, GATPEDLNQKL, GLYEWGGARI, and FDKEWNLIEQN, binding to the same site of the hypervariable region of, the anti-p24 (HIV-1) monoclonal antibody CB4-1. Conversion of these, peptides into each other could be achieved in nine or 10 single amino acid, substitution steps without loss of antibody binding. Such pathways were, identified by analyzing all 7 620 480 pathways connecting 2560 different, peptides, and testing them for CB4-1 binding. The binding modes of, intermediate peptides of selected optimal pathways were characterized, using complete sets of substitution analogs, revealing that a number of, sequential substitutions accumulated without changing the pattern of key, interacting residues. At a distinct step, however, one single amino acid, exchange induces a sudden change in the binding mode, indicating a flip in, specificity and conformation. Our data represent a model of how different, specificities, structures and functions might evolve in protein-protein, recognition.
About this Structure
1HH9 is a Protein complex structure of sequences from Mus musculus with as ligand. Full crystallographic information is available from OCA.
Reference
Evolutionary transition pathways for changing peptide ligand specificity and structure., Hoffmuller U, Knaute T, Hahn M, Hohne W, Schneider-Mergener J, Kramer A, EMBO J. 2000 Sep 15;19(18):4866-74. PMID:10990450
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