2b1h: Difference between revisions
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<StructureSection load='2b1h' size='340' side='right'caption='[[2b1h]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2b1h' size='340' side='right'caption='[[2b1h]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2b1h]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2b1h]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B1H FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2b1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b1h OCA], [https://pdbe.org/2b1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b1h RCSB], [https://www.ebi.ac.uk/pdbsum/2b1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b1h ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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==See Also== | ==See Also== | ||
*[[Antibody 3D structures|Antibody 3D structures]] | *[[Antibody 3D structures|Antibody 3D structures]] | ||
*[[3D structures of human antibody|3D structures of human antibody]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Gorny | [[Category: Gorny MK]] | ||
[[Category: Stanfield | [[Category: Stanfield RL]] | ||
[[Category: Wilson | [[Category: Wilson IA]] | ||
[[Category: Zolla-Pazner | [[Category: Zolla-Pazner S]] | ||
Latest revision as of 10:32, 23 August 2023
Crystal structure analysis of anti-HIV-1 V3 Fab 2219 in complex with UG29 peptideCrystal structure analysis of anti-HIV-1 V3 Fab 2219 in complex with UG29 peptide
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHuman monoclonal antibody 2219 is a neutralizing antibody isolated from a human immunodeficiency virus type 1-infected individual. 2219 was originally selected for binding to a V3 fusion protein and can neutralize primary isolates from subtypes B, A, and F. Thus, 2219 represents a cross-reactive, human anti-V3 antibody. Fab 2219 binds to one face of the variable V3 beta-hairpin, primarily contacting conserved residues on the N-terminal beta-strand of V3, leaving the V3 crown or tip largely accessible. Three V3/2219 complexes reveal the antibody-bound conformations for both the N- and C-terminal regions that flank the V3 crown and illustrate how twisting of the V3 loop alters the relative dispositions and pairing of the amino acids in the adjacent V3 beta-strands and how the antibody can accommodate V3 loops with different sequences. Crystal structures of human immunodeficiency virus type 1 (HIV-1) neutralizing antibody 2219 in complex with three different V3 peptides reveal a new binding mode for HIV-1 cross-reactivity.,Stanfield RL, Gorny MK, Zolla-Pazner S, Wilson IA J Virol. 2006 Jun;80(12):6093-105. PMID:16731948[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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