Introduction Numbering Sequences Structures Modelling Macros Publications Links
Homology Modelling CDR Grafting Examples HuCAL Biophysical Properties Randomization Catalytic Antibodies

HuCal VH5 Problem Spots

Display all
Display backbone only
Display as spacefilling
Display as Sticks
Color by atom type
Color by residue type
Highlight charges
CDRs VH
positive Phi angles
cis/trans Pro residues
H-Bonds
V/C interf. VH
Core residues VH
Dimer interf. VH Haptens
Dimer interf. VH Oligom.
Dimer interf. VH Proteins
Antigen interf. VH Haptens
Antigen interf. VH Oligom.
Antigen interf. VH Proteins
Randomized residues VH
Arg H108 - Asp H137
H5: Val->Thr
exposed hydrophobic residue
H12: Val->Asp
exposed hydrophobic residue
4/4/20: H12 Leu-> Asn (+), H12 Leu -> Asp (++) %sol (L.Nieba)
4D5Flu: Ser selected from (L S D N F Y P H I T V A) (S.Jung)
No data on how it would affect FAB format
H47: Met->Ala exposed hydrophobic residue
H77: Gln->Arg
conserved charge interaction with H100 Asp, even Lys->Arg results in significant stabilization
(compensating for loss of VL disulfide bond in ab48), H77 Arg->Lys destabilizing in GCN4, H77 Lys->Arg improves production in His
H86: Ile->Ser exposed hydrophobic residue
H103: Met->Thr
exposed hydrophobic residue
4/4/20: H90 Val -> Ser, H93 Met -> Ser and H95 Ile -> Ser (++) %sol. (L.Nieba)
Caution:
Lateral interaction with Leu H144 may have a stabilizing effect, which would be lost upon substitution with a small hydrophilic residue
No data on how it would affect FAB format
H144: Leu->Thr
exposed hydrophobic residue
4D5Flu: Ser not conterselected from LS (S.Jung)
Caution:
Lateral interaction with Val H103 may have a stabilizing effect, which would be lost upon substitution with a small hydrophilic residue
No data on how it would affect FAB format

HuCal Structure Display VH 5

Select Structure to display:
AAAAA Homepage Zürich University Dept. of Biochemistry Plückthun Group Annemarie Honegger

Last Modified by A.Honegger Tuesday, March 25, 2008