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MOLECULAR AND CELLULAR BIOLOGY .4 publication o_ tl_ Amerfcan Society lot MicrobfoMg'y Manuscript

Date: 21 Dec 1992
Length: 13 pages

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nysa_ctr1 40000027-40000039

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
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.
Date Loaded
11 Jan 2006
Box
0001

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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
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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.). REFERF.~CES 40000038
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