NYSA CTR 1
MOLECULAR AND CELLULAR BIOLOGY .4 publication o_ tl_ Amerfcan Society lot MicrobfoMg'y Manuscript
Abstract
Title: "A unique ribonucleoprotein complex..."
Fields
- Named Organization
- American Cancer Society
- Loyola University (Montreal) (Became Concordia University (Montreal))
Merged with Sir George Williams University to form Concordia University.- Loyola University Chicago
- March of Dimes (Voluntary health organzation concerned with birth defects)
- National Institutes of Health
- National Institutes of Health (NIH)
- National Science Foundation
- University Medical Center
- University of California at San Francisco
- University of Virginia
- Loyola University (Montreal) (Became Concordia University (Montreal))
- Named Person
- Amero, Sally A.
- Beyer, Ann L.
- Cass, Cynthia L.
- Kretsinger, Robert H.
- Miller, Oscar L., Jr.
- Pearson, William R.
- Weiner, Alan M.
- Yamamoto, Keith R.
- Beyer, Ann L.
- Date Loaded
- 11 Jan 2006
- Box
- 0001
Document Images
PPAR
tll
DAF
hFR mGR
tAR ~GR
ECR
hVDR
-IR3
R HNF-4
X
hRXR o˘
˘COUP
h.ear-2 ARP-1
K hTR25 h.ear-3 svpA
NAK
NGR-B
nur/T?
40000037

Me L E,'~CO - 1 ~.~2
Vo~, 6 ~',~.3.1
6
Zn finger domain
0 25% 50% 75% 95%
0 100 200 400 800
Fig. 2. Similarity Matrices for the DNA-Bindlng Oomalns and Ligand-Binding Domains in Nuclear
Receptor Proteins
Similarity scores were calculated from either the DNA-blnding domain or the Ilgand-bincling
domain sequences for each pair of
nuclear receptors using the Smith-Waterman algorithm (7). The value plotted for the DNAJoinding
domalns Is percent similarity (see
text). Some of the DNA-bInding domains are described in the legend to Fig. 1; the additional,
nonidentical ones are described
below. The raw s~ilarity scores were used for the matrix representation of the Ilgand-binding
domains. The ligand-bincling domain
sequences included a~l amino acid residues from the encl of the DNA-binding domain to the C-terminus
of the protein. Sequences
for the ligand-b|nding domains of the cVDR, ECR, DAF, nRAR, end DHR3 proteins were not available,
and these receptors were
not included in thls analysis. The additional receptors and the~r sources are: hTR(x2, human thyrold
receptor-=2 (#A30893); rTR=J,
rat thyroid receptoro=l ($RATTHR); h-ear-7, human esr-7 gene product (#B32286); erb62, rat thyroid
receptor (#A31820); rTR,
rat thyroid receptor (#A30226); mRAR=, mouse ret~nolc acid receptor-= (#S05052); mRART=, mouse
retinolc acid receptor--/=
(#A35991); mRAR3"~, mc4Jse ret~no[c acid receptor-of~ (35); hl:~R~, human retino~c ec{d receptoro~
(#S02827); mRAR#, mouse
retinoic acid receptoro/~'(#S05051 }; rbPR, rabbit progesterone receptor (#A25923); cFR, chicken
progesterone receptor (#S06284);
rGR, rat glucocorticoid receptor (#ORRTG); mGRc~, mouse glucoco~coid receptor-= (#S02212); rER, rat
estrogen receptor
(#S07379); cER, chicken estrogen receptor ($GHKERR); rVDRo rat vitamin D receptor (#A31761); svpB,
Drosophila seven-up
germs product B (-#B32693); hTR290 human thyroid-related receptor 29 ($HUMTR29); ~nd hTR211, human
thyroid-related receptor
211 ($HU?,TrR211).
~nce of the nut!ear receptor precurs(:r, naturrJ se,~tion
has retained the configuration of DNA-b!ndlng damon
w;th cognate I,~gand-binding demon because damon
shut,rig or loss would produce unde~.~rab!e phys[o!og-
ica] consequences.
Acknowted_qments
° Present address: D~pa.rtment (~f Molacul3r and Ce.,tulat
Blcche~st~y, LoyoI~ Un:vers~ty Med!cal Center, Maywood,
Th~s wof~ w~s supported by NIH Grant 5-S07-RR-05431-
28 and Amer'c'~J1 C~cer Society Grant IN 149F
N]H Grant GM-39271 (to At~n L. Bsy~r), NASA Gr'a~t NAGW-
1233 (to R.H.K.), NSF Grant DM~-8"/16787 (to K.R.Y.), and
NIH Grant LM-04969 (to W.R.P.).
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