CRYSTAL STRUCTURE OF HUMAN ANGIOGENIN IN COMPLEX WITH FAB FRAGMENT OF ITS MONOCLONAL ANTIBODY MAB 26-2F


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B-Cell Epitope
Epitope  
   
Complex PDB ID 1H0D
Accession Number 3DIEP0130
IEDB ID 77533
Epitope Sequence G58; L59; S61; P62; C63; K64; D65; G109; G110; S111; P112; W113; P114; P115
Starting Position58-59,61-65,109
Ending Position115
Epitope Type Discontinuous Epitope

Assay Information  
Assay Antigen Angiogenin precursor Angiogenin precursor Homo sapiens
PDB CategoryIMMUNE SYSTEM/HYDROLASE
Keyword IMMUNE SYSTEM/HYDROLASE; COMPLEX (ANTIBODY/HYDROLASE); RIBONUCLEASE; ANTIBODY
Antibody Residues Interacting with Antigen Open in new window      Download dimplot pdb file
Antibody Chain 1 PDB Chain B
Antibody Chain 2 PDB ChainA
Antigen PDB ChainC
Contact Area for Antigen 682.1
Contact Area for Antibody628
CommentsComparison of angiogenin (123 aa) in complex with Fab (this structure) with the structure of free angiogenin [PDB: 1B1I] revealed that antibody binding induces dramatic conformational changes in the cell binding region of angiogenin at the opposite end of the molecule from the antibody binding site. The epitope is located at two loops comprising residues 34-41 and 85-91. Their conformation does not change upon antibody binding. Residues 59-68 comprise the cell binding region. They change their conformation dramatically; Rmsd for ten Ca atoms is 13.2 Angstrom. In free angiogenin; residues 62-68 are part of a ß-hairpin formed by ß-strands 2 and 3 and the intervening loop 66-68 residues 59-61 lie on a loop that connects the hairpin structure with a-helix 3. In the complex; the ß-strand 2 is lost; and the entire 58-67 segment forms a loop that extends much further out from the rest of the molecule than does ß-hairpin. The authors show that antibody binding; not crystal packing; induces the conformational change. The native conformation is critical for the interaction of angiogenin with surface components on its endothelial cell targets. Antibody binding disables angiogenin by destroying the native conformation of the cell binding region.

Experimental Details
Method
X-RAY DIFFRACTION
Resolution
2
R-Value
0.232
Space Group
C 1 2 1
Unit Cell
Length(Å) Angle(°)
a = 120.58 α = 90
b = 72.53 β = 112.46
c = 86.99 γ = 90


Source Information  
Structure Determination Method X-RAY DIFFRACTION


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Ligand
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