1xow: Difference between revisions

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[[Image:1xow.gif|left|200px]]<br />

[[Image:1xow.gif|left|200px]]<br /><applet load="1xow" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1xow" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1xow, resolution 1.80Å" />

'''Crystal structure of the human androgen receptor ligand binding domain bound with an androgen receptor NH2-terminal peptide, AR20-30, and R1881'''<br />

==Overview==

The androgen receptor (AR) is required for male sex development and, contributes to prostate cancer cell survival. In contrast to other nuclear, receptors that bind the LXXLL motifs of coactivators, the AR ligand, binding domain is preferentially engaged in an interdomain interaction, with the AR FXXLF motif. Reported here are crystal structures of the, ligand-activated AR ligand binding domain with and without bound FXXLF and, LXXLL peptides. Key residues that establish motif binding specificity are, identified through comparative structure-function and mutagenesis studies., A mechanism in prostate cancer is suggested by a functional AR mutation at, a specificity-determining residue that recovers coactivator LXXLL motif, binding. An activation function transition hypothesis is proposed in which, an evolutionary decline in LXXLL motif binding parallels expansion and, functional dominance of the NH(2)-terminal transactivation domain in the, steroid receptor subfamily.

The androgen receptor (AR) is required for male sex development and contributes to prostate cancer cell survival. In contrast to other nuclear receptors that bind the LXXLL motifs of coactivators, the AR ligand binding domain is preferentially engaged in an interdomain interaction with the AR FXXLF motif. Reported here are crystal structures of the ligand-activated AR ligand binding domain with and without bound FXXLF and LXXLL peptides. Key residues that establish motif binding specificity are identified through comparative structure-function and mutagenesis studies. A mechanism in prostate cancer is suggested by a functional AR mutation at a specificity-determining residue that recovers coactivator LXXLL motif binding. An activation function transition hypothesis is proposed in which an evolutionary decline in LXXLL motif binding parallels expansion and functional dominance of the NH(2)-terminal transactivation domain in the steroid receptor subfamily.

==Disease==

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==About this Structure==

1XOW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with R18 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1XOW OCA].

1XOW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=R18:'>R18</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XOW OCA].

==Reference==

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[[Category: An, G.]]

[[Category: He, B.]]

[[Category: Hnat, A.T.]]

[[Category: Hnat, A T.]]

[[Category: Jr., R.T.Gampe.]]

[[Category: Jr., R T.Gampe.]]

[[Category: Kalman, R.I.]]

[[Category: Kalman, R I.]]

[[Category: Kole, A.J.]]

[[Category: Kole, A J.]]

[[Category: Minges, J.T.]]

[[Category: Minges, J T.]]

[[Category: Stanley, T.B.]]

[[Category: Stanley, T B.]]

[[Category: Stewart, E.L.]]

[[Category: Stewart, E L.]]

[[Category: Wilson, E.M.]]

[[Category: Wilson, E M.]]

[[Category: R18]]

[[Category: crystal structure; human androgen receptor ligand binding domain; androgen receptor nh2-terminal peptide ar20-30; r1881]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 20~~:08:~~53 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:57:03 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1xow.gif|left|200px]]<br />
+[[Image:1xow.gif|left|200px]]<br /><applet load="1xow" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1xow" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1xow, resolution 1.80&Aring;" />
 '''Crystal structure of the human androgen receptor ligand binding domain bound with an androgen receptor NH2-terminal peptide, AR20-30, and R1881'''<br />
 ==Overview==
-The androgen receptor (AR) is required for male sex development and, contributes to prostate cancer cell survival. In contrast to other nuclear, receptors that bind the LXXLL motifs of coactivators, the AR ligand, binding domain is preferentially engaged in an interdomain interaction, with the AR FXXLF motif. Reported here are crystal structures of the, ligand-activated AR ligand binding domain with and without bound FXXLF and, LXXLL peptides. Key residues that establish motif binding specificity are, identified through comparative structure-function and mutagenesis studies., A mechanism in prostate cancer is suggested by a functional AR mutation at, a specificity-determining residue that recovers coactivator LXXLL motif, binding. An activation function transition hypothesis is proposed in which, an evolutionary decline in LXXLL motif binding parallels expansion and, functional dominance of the NH(2)-terminal transactivation domain in the, steroid receptor subfamily.
+The androgen receptor (AR) is required for male sex development and contributes to prostate cancer cell survival. In contrast to other nuclear receptors that bind the LXXLL motifs of coactivators, the AR ligand binding domain is preferentially engaged in an interdomain interaction with the AR FXXLF motif. Reported here are crystal structures of the ligand-activated AR ligand binding domain with and without bound FXXLF and LXXLL peptides. Key residues that establish motif binding specificity are identified through comparative structure-function and mutagenesis studies. A mechanism in prostate cancer is suggested by a functional AR mutation at a specificity-determining residue that recovers coactivator LXXLL motif binding. An activation function transition hypothesis is proposed in which an evolutionary decline in LXXLL motif binding parallels expansion and functional dominance of the NH(2)-terminal transactivation domain in the steroid receptor subfamily.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-XOW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with R18 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XOW OCA].
+XOW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=R18:'>R18</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XOW OCA].
 ==Reference==
@@ Line 19: / Line 18: @@
 [[Category: An, G.]]
 [[Category: He, B.]]
-[[Category: Hnat, A.T.]]
+[[Category: Hnat, A T.]]
-[[Category: Jr., R.T.Gampe.]]
+[[Category: Jr., R T.Gampe.]]
-[[Category: Kalman, R.I.]]
+[[Category: Kalman, R I.]]
-[[Category: Kole, A.J.]]
+[[Category: Kole, A J.]]
-[[Category: Minges, J.T.]]
+[[Category: Minges, J T.]]
-[[Category: Stanley, T.B.]]
+[[Category: Stanley, T B.]]
-[[Category: Stewart, E.L.]]
+[[Category: Stewart, E L.]]
-[[Category: Wilson, E.M.]]
+[[Category: Wilson, E M.]]
 [[Category: R18]]
 [[Category: crystal structure; human androgen receptor ligand binding domain; androgen receptor nh2-terminal peptide ar20-30; r1881]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:08:53 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:57:03 2008''