1bsx: Difference between revisions

Line 1:

[[Image:1bsx.~~gif~~|left|200px]]

[[Image:1bsx.png|left|200px]]

<!--

Line 9:

Line 10:

~~'''~~STRUCTURE AND SPECIFICITY OF NUCLEAR RECEPTOR-COACTIVATOR INTERACTIONS~~'''~~

===STRUCTURE AND SPECIFICITY OF NUCLEAR RECEPTOR-COACTIVATOR INTERACTIONS===

~~==Overview==~~

<!--

Combinatorial regulation of transcription implies flexible yet precise assembly of multiprotein regulatory complexes in response to signals. Biochemical and crystallographic analyses revealed that hormone binding leads to the formation of a hydrophobic groove within the ligand binding domain (LBD) of the thyroid hormone receptor that interacts with an LxxLL motif-~~containing alpha~~-~~helix from GRIP1~~, ~~a coactivator. Residues immediately adjacent~~ to the ~~motif modulate the affinity of the interaction; the motif and the adjacent sequences are employed to different extents in binding to different receptors~~. ~~Such interactions of amphipathic alpha-helices with hydrophobic grooves define protein interfaces in other regulatory complexes as well~~. ~~We suggest that these common structural elements impart flexibility to combinatorial regulation~~, ~~whereas side chains at~~ the ~~interface impart specificity~~.

The line below this paragraph, {{ABSTRACT_PUBMED_9808622}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9808622 is the PubMed ID number.

-->

==About this Structure==

Line 34:

Line 38:

[[Category: Nuclear receptor]]

[[Category: Specificity interaction site]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 11~~:55:08 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:40:25 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1bsx.gif|left|200px]]
+{{Seed}}
+[[Image:1bsx.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1bsx|  PDB=1bsx  |  SCENE=  }}
-'''STRUCTURE AND SPECIFICITY OF NUCLEAR RECEPTOR-COACTIVATOR INTERACTIONS'''
+===STRUCTURE AND SPECIFICITY OF NUCLEAR RECEPTOR-COACTIVATOR INTERACTIONS===
-==Overview==
+<!--
-Combinatorial regulation of transcription implies flexible yet precise assembly of multiprotein regulatory complexes in response to signals. Biochemical and crystallographic analyses revealed that hormone binding leads to the formation of a hydrophobic groove within the ligand binding domain (LBD) of the thyroid hormone receptor that interacts with an LxxLL motif-containing alpha-helix from GRIP1, a coactivator. Residues immediately adjacent to the motif modulate the affinity of the interaction; the motif and the adjacent sequences are employed to different extents in binding to different receptors. Such interactions of amphipathic alpha-helices with hydrophobic grooves define protein interfaces in other regulatory complexes as well. We suggest that these common structural elements impart flexibility to combinatorial regulation, whereas side chains at the interface impart specificity.
+The line below this paragraph, {{ABSTRACT_PUBMED_9808622}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9808622 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9808622}}
 ==About this Structure==
@@ Line 34: / Line 38: @@
 [[Category: Nuclear receptor]]
 [[Category: Specificity interaction site]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:55:08 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:40:25 2008''