This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2h6w

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2h6w.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2h6w.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2h6w| PDB=2h6w | SCENE= }}
{{STRUCTURE_2h6w| PDB=2h6w | SCENE= }}
-
'''Thyroid hormone receptor bound to T3'''
+
===Thyroid hormone receptor bound to T3===
-
==Overview==
+
<!--
-
The thyroid hormone receptor (TR) D-domain links the ligand-binding domain (LBD, EF-domain) to the DNA-binding domain (DBD, C-domain), but its structure, and even its existence as a functional unit, are controversial. The D domain is poorly conserved throughout the nuclear receptor family and was originally proposed to comprise an unfolded hinge that facilitates rotation between the LBD and the DBD. Previous TR LBD structures, however, have indicated that the true unstructured region is three to six amino acid residues long and that the D-domain N terminus folds into a short amphipathic alpha-helix (H0) contiguous with the DBD and that the C terminus of the D-domain comprises H1 and H2 of the LBD. Here, we solve structures of TR-LBDs in different crystal forms and show that the N terminus of the TRalpha D-domain can adopt two structures; it can either fold into an amphipathic helix that resembles TRbeta H0 or form an unstructured loop. H0 formation requires contacts with the AF-2 coactivator-binding groove of the neighboring TR LBD, which binds H0 sequences that resemble coactivator LXXLL motifs. Structural analysis of a liganded TR LBD with small angle X-ray scattering (SAXS) suggests that AF-2/H0 interactions mediate dimerization of this protein in solution. We propose that the TR D-domain has the potential to form functionally important extensions of the DBD and LBD or unfold to permit TRs to adapt to different DNA response elements. We also show that mutations of the D domain LXXLL-like motif indeed selectively inhibit TR interactions with an inverted palindromic response element (F2) in vitro and TR activity at this response element in cell-based transfection experiments.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16781732}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16781732 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16781732}}
==About this Structure==
==About this Structure==
Line 42: Line 46:
[[Category: Thyroid]]
[[Category: Thyroid]]
[[Category: Tr]]
[[Category: Tr]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:56:24 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:06:54 2008''

Revision as of 11:06, 27 July 2008

Image:2h6w.png

Template:STRUCTURE 2h6w

Thyroid hormone receptor bound to T3

Template:ABSTRACT PUBMED 16781732

About this Structure

2H6W is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural rearrangements in the thyroid hormone receptor hinge domain and their putative role in the receptor function., Nascimento AS, Dias SM, Nunes FM, Aparicio R, Ambrosio AL, Bleicher L, Figueira AC, Santos MA, de Oliveira Neto M, Fischer H, Togashi M, Craievich AF, Garratt RC, Baxter JD, Webb P, Polikarpov I, J Mol Biol. 2006 Jul 14;360(3):586-98. Epub 2006 May 19. PMID:16781732

Page seeded by OCA on Sun Jul 27 14:06:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2h6w"
Personal tools