6n32: Difference between revisions
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==Anti-HIV-1 Fab 2G12 re-refinement== | ==Anti-HIV-1 Fab 2G12 re-refinement== | ||
<StructureSection load='6n32' size='340' side='right' caption='[[6n32]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='6n32' size='340' side='right'caption='[[6n32]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6n32]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1om3 1om3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N32 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6N32 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6n32]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1om3 1om3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N32 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6N32 FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 6n32" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6n32" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Antibody 3D structures|Antibody 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Calarese, D A]] | [[Category: Calarese, D A]] | ||
[[Category: Stanfield, R L]] | [[Category: Stanfield, R L]] |
Revision as of 14:33, 1 January 2020
Anti-HIV-1 Fab 2G12 re-refinementAnti-HIV-1 Fab 2G12 re-refinement
Structural highlights
Publication Abstract from PubMedHuman antibody 2G12 neutralizes a broad range of human immunodeficiency virus type 1 (HIV-1) isolates by binding an unusually dense cluster of carbohydrate moieties on the "silent" face of the gp120 envelope glycoprotein. Crystal structures of Fab 2G12 and its complexes with the disaccharide Manalpha1-2Man and with the oligosaccharide Man9GlcNAc2 revealed that two Fabs assemble into an interlocked VH domain-swapped dimer. Further biochemical, biophysical, and mutagenesis data strongly support a Fab-dimerized antibody as the prevalent form that recognizes gp120. The extraordinary configuration of this antibody provides an extended surface, with newly described binding sites, for multivalent interaction with a conserved cluster of oligomannose type sugars on the surface of gp120. The unique interdigitation of Fab domains within an antibody uncovers a previously unappreciated mechanism for high-affinity recognition of carbohydrate or other repeating epitopes on cell or microbial surfaces. Antibody domain exchange is an immunological solution to carbohydrate cluster recognition.,Calarese DA, Scanlan CN, Zwick MB, Deechongkit S, Mimura Y, Kunert R, Zhu P, Wormald MR, Stanfield RL, Roux KH, Kelly JW, Rudd PM, Dwek RA, Katinger H, Burton DR, Wilson IA Science. 2003 Jun 27;300(5628):2065-71. PMID:12829775[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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