View source for 1bog

==ANTI-P24 (HIV-1) FAB FRAGMENT CB41 COMPLEXED WITH AN EPITOPE-HOMOLOGOUS PEPTIDE==
<StructureSection load='1bog' size='340' side='right' caption='[[1bog]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bog]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BOG FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bog OCA], [http://pdbe.org/1bog PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bog RCSB], [http://www.ebi.ac.uk/pdbsum/1bog PDBsum]</span></td></tr>
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== 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/bo/1bog_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf].
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== Publication Abstract from PubMed ==
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.

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<ref>PMID:9413990</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1bog" style="background-color:#fffaf0;"></div>

==See Also==
*[[Monoclonal Antibody|Monoclonal Antibody]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Mus musculus]]
[[Category: Hoehne, W]]
[[Category: Keitel, T]]
[[Category: Kramer, A]]
[[Category: Schneider-Mergener, J]]
[[Category: Scholz, C]]
[[Category: Wessner, H]]
[[Category: Cross reactivity]]
[[Category: Fab-fragment]]
[[Category: Hiv-1]]
[[Category: Polyspecificity]]