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.


1k4w

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1k4w.gif|left|200px]]<br /><applet load="1k4w" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1k4w.gif|left|200px]]
-
caption="1k4w, resolution 1.90&Aring;" />
+
 
-
'''X-ray structure of the orphan nuclear receptor ROR beta ligand-binding domain in the active conformation'''<br />
+
{{Structure
 +
|PDB= 1k4w |SIZE=350|CAPTION= <scene name='initialview01'>1k4w</scene>, resolution 1.90&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=STE:STEARIC ACID'>STE</scene>
 +
|ACTIVITY=
 +
|GENE= NR1F2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
 +
}}
 +
 
 +
'''X-ray structure of the orphan nuclear receptor ROR beta ligand-binding domain in the active conformation'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1K4W is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=STE:'>STE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K4W OCA].
+
1K4W is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K4W OCA].
==Reference==
==Reference==
-
X-ray structure of the orphan nuclear receptor RORbeta ligand-binding domain in the active conformation., Stehlin C, Wurtz JM, Steinmetz A, Greiner E, Schule R, Moras D, Renaud JP, EMBO J. 2001 Nov 1;20(21):5822-31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11689423 11689423]
+
X-ray structure of the orphan nuclear receptor RORbeta ligand-binding domain in the active conformation., Stehlin C, Wurtz JM, Steinmetz A, Greiner E, Schule R, Moras D, Renaud JP, EMBO J. 2001 Nov 1;20(21):5822-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11689423 11689423]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
Line 25: Line 34:
[[Category: transcriptionally active conformation]]
[[Category: transcriptionally active conformation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:30:10 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:12:37 2008''

Revision as of 10:12, 20 March 2008


PDB ID 1k4w

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands:
Gene: NR1F2 (Rattus norvegicus)
Coordinates: save as pdb, mmCIF, xml



X-ray structure of the orphan nuclear receptor ROR beta ligand-binding domain in the active conformation


Overview

The retinoic acid-related orphan receptor beta (RORbeta) exhibits a highly restricted neuronal-specific expression pattern in brain, retina and pineal gland. So far, neither a natural RORbeta target gene nor a functional ligand have been identified, and the physiological role of the receptor is not well understood. We present the crystal structure of the ligand-binding domain (LBD) of RORbeta containing a bound stearate ligand and complexed with a coactivator peptide. In the crystal, the monomeric LBD adopts the canonical agonist-bound form. The fatty acid ligand-coactivator peptide combined action stabilizes the transcriptionally active conformation. The large ligand-binding pocket is strictly hydrophobic on the AF-2 side and more polar on the beta-sheet side where the carboxylate group of the ligand binds. Site-directed mutagenesis experiments validate the significance of the present structure. Homology modeling of the other isotypes will help to design isotype-selective agonists and antagonists that can be used to characterize the physiological functions of RORs. In addition, our crystallization strategy can be extended to other orphan nuclear receptors, providing a powerful tool to delineate their functions.

About this Structure

1K4W is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

X-ray structure of the orphan nuclear receptor RORbeta ligand-binding domain in the active conformation., Stehlin C, Wurtz JM, Steinmetz A, Greiner E, Schule R, Moras D, Renaud JP, EMBO J. 2001 Nov 1;20(21):5822-31. PMID:11689423

Page seeded by OCA on Thu Mar 20 12:12:37 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools