1op3
From Proteopedia
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|PDB= 1op3 |SIZE=350|CAPTION= <scene name='initialview01'>1op3</scene>, resolution 1.75Å | |PDB= 1op3 |SIZE=350|CAPTION= <scene name='initialview01'>1op3</scene>, resolution 1.75Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1om3|1OM3]], [[1op5|1OP5]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1op3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1op3 OCA], [http://www.ebi.ac.uk/pdbsum/1op3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1op3 RCSB]</span> | ||
}} | }} | ||
| Line 35: | Line 38: | ||
[[Category: Wilson, I A.]] | [[Category: Wilson, I A.]] | ||
[[Category: Zwick, M B.]] | [[Category: Zwick, M B.]] | ||
| - | [[Category: | + | [[Category: anti-carbohydrate antibody]] |
| - | + | [[Category: domain-swapped fab 2g12]] | |
| - | [[Category: domain-swapped fab 2g12 | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:48:23 2008'' |
Revision as of 19:48, 30 March 2008
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| , resolution 1.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1OM3, 1OP5
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Fab 2G12 bound to Man1->2Man
Overview
Human 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.
About this Structure
1OP3 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
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