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Modifications and Mutagenesis

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VDR: Mutation & Modification Data / (13-Oct-99)

A. Mutations in the LBD.
This table lists all mutations known from the literature or from informal communication up to the date given above. Complete citations are given in the Bibliography. Highlighting indicates mutations deemed most relevant to 1,25-(OH)2-D3 binding.
ChangeEffectReference
C190W* familial VDRR-II Thompson et al. (1991)
S225A Kd for ligand unchanged Väisänen et al. (1998)
H229A Kd for ligand increased by 27X Väisänen et al. (1998)
D232A Kd for ligand increased by 30X Väisänen et al. (1998)
L233?
V234A Kd for ligand almost unchanged Väisänen et al. (1998)
S235A Kd for ligand almost unchanged Väisänen et al. (1998)
Y236A Kd for ligand increased by 3.5X Väisänen et al. (1998)
S237A Kd for ligand increased by 27X Väisänen et al. (1998)
K240A Kd for ligand almost unchanged Väisänen et al. (1998)
I242A Kd for ligand almost unchanged Väisänen et al. (1998)
F244G impaired transactivation Whitfield et al. (1995)
K246A Kd for ligand increased by 2X Väisänen et al. (1998)
K246R
L254G impaired transactivation; no RXR heterodimer formed Whitfield et al. (1995)
Q259P dimerization (w/ RXR) inhibited
R274L* ligand binding severely decreased; VDRR-II Kristjansson et al. (1993)
S275A Kd for ligand increased by 5.3X Väisänen et al. (1998)
M284A ligand binding 50% of WT (unpublished) Ray, Swamy (1999)
M284S ligand binding 60% of WT
W286A no ligand binding (unpublished) Ray, Swamy (1999)
W286F no ligand binding
C288G ligand binding "attenuated severely" at 37 ° C; decreased 3X at 4 ° C; VDRR-II Nakajima et al. (1996)
Y295STOP* no ligand binding Ritchie et al. (1989)
H305Q* ligand binding decreased 5X Malloy et al. (1997)
I314S* reduced transactivation; high ligand conc. restores it; RXR interaction diminished Whitfield et al. (1996)
C337G ligand binding moderately decreased at 37 ° C Nakajima et al. (1996)
C369G ligand binding only mildly affected at 37 ° C Nakajima et al. (1996)
K386Q very slight decrease in ligand binding Masuyama et al. (1997)
L387STOP no ligand binding detectable Masuyama et al. (1997)
R391C* transactivation decreased together with RXR binding Whitfield et al. (1996)
H397?
L404STOP Kd for ligand increased by 10X Masuyama et al. (1997)
L417A no change in ligand binding; transcriptional activation gone Jurutka et al. (1997)
L417S ligand binding normal; transactivation abolished (also coactivator binding) Masuyama et al. (1997)
V418 contacts ligand?
E420A no change in ligand binding; transcriptional activation gone Jurutka et al. (1997)
E420Q ligand binding normal; transactivation abolished (also coactivator binding) Masuyama et al. (1997)
F422 contacts ligand?
E425Q no effect on ligand binding or transactivation Masuyama et al. (1997)
B. Mutations in the DBD
ChangeEffectReference
G33D
H35Q
K45E
G46D
F47I
R50Q
R73Q
R80Q
C. Modifications
1. Proteolysis
2. Affinity labeling
3. Photoaffinity labeling

3-bromoacetyl-1,25-(OH)2-D3
Other modifications?
Site-directed mutants
Created in the Ray laboratory
From literature



Sean Quinlan <wwwadmin@darwin.bu.edu>
last modified: Saturday, October 30, 1999 11:04:54 AM