spacer
spacer

PDBsum entry 1flr

Go to PDB code: 
Top Page protein ligands Protein-protein interface(s) links
Immunoglobulin PDB id
1flr
Contents
Protein chains
219 a.a. *
216 a.a. *
Ligands
FLU
Waters ×292
* Residue conservation analysis

References listed in PDB file
Key reference
Title 1.85 a structure of anti-Fluorescein 4-4-20 FAB.
Authors M.Whitlow, A.J.Howard, J.F.Wood, E.W.Voss, K.D.Hardman.
Ref. Protein Eng, 1995, 8, 749-761.
PubMed id 8637844
Note In the PDB file this reference is annotated as "TO BE PUBLISHED". The citation details given above were identified by an automated search of PubMed on title and author names, giving a percentage match of 85%.
Abstract
The crystal complex of fluorescein bound to the high-affinity anti-fluorescein 4-4-20 Fab (Ka = 10(10) M-1 at 2 degrees C) has been determined at 1.85 A. Isomorphous crystals of two isoelectric forms (pI = 7.5 and 7.9) of the anti-fluorescein 4-4-20 Fab, an IgG2A [Gibson et al. (1988) Proteins: Struct. Funct. Genet., 3, 155-160], have been grown. Both complexes crystallize with one molecule in the asymmetric unit in space group P1, with a = 42.75 A, b = 43.87 A, c = 58.17 A, alpha = 95.15 degrees, beta = 86.85 degrees and gamma = 98.01 degrees. The final structure has an R value of 0.188 at 1.85 A resolution. Interactions between bound fluorescein, the complementarity-determining regions (CDRs) of the Fab and the active-site mutants of the 4-4-20 single-chain Fv will be discussed. Differences were found between the structure reported here and the previously reported 2.7 A 4-4-20 Fab structure [Herron et al. (1989) Proteins: Struct. Funct. Genet., 5, 271-280]. Our structure determination was based on 26,328 unique reflections--four times the amount of data used in the previous report. Differences in the two structures could be explained by differences in interpreting the electron density maps at the various resolutions. The r.m.s. deviations between the variable and constant domains of the two structures were 0.77 and 1.54 A, respectively. Four regions of the light chain and four regions of the heavy chain had r.m.s. backbone deviations of > 4 A. The most significant of these was the conformation of the light chain CDR 1.
Secondary reference #1
Title Three-Dimensional structure of a fluorescein-Fab complex crystallized in 2-Methyl-2,4-Pentanediol.
Authors J.N.Herron, X.M.He, M.L.Mason, E.W.Voss, A.B.Edmundson.
Ref. Proteins, 1989, 5, 271-280.
PubMed id 2508085
Abstract
Secondary reference #2
Title Differences in crystal properties and ligand affinities of an antifluorescyl FAB (4-4-20) in two solvent systems.
Authors A.L.Gibson, J.N.Herron, X.M.He, V.A.Patrick, M.L.Mason, J.N.Lin, D.M.Kranz, E.W.Voss, A.B.Edmundson.
Ref. Proteins, 1988, 3, 155-160.
PubMed id 3255103
Abstract
Secondary reference #3
Title Comparison of variable region primary structures within an anti-Fluorescein idiotype family.
Authors W.D.Bedzyk, L.S.Johnson, G.S.Riordan, E.W.Voss.
Ref. J Biol Chem, 1989, 264, 1565-1569.
PubMed id 2492278
Abstract
PROCHECK
Go to PROCHECK summary
 Headers

 

spacer

spacer