2lbd: Difference between revisions

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==Overview==

The 2.0-A crystal structure of the ligand-binding domain (LBD) of the, human retinoic acid receptor (RAR)-gamma bound to all-trans retinoic acid, reveals the ligand-binding interactions and suggests an electrostatic, guidance mechanism. The overall fold is similar to that of the human, RXR-alpha apo-LBD, except for the carboxy-terminal part which folds back, towards the LBD core, contributing to the hydrophobic ligand pocket and, 'sealing' its entry site. We propose a 'mouse trap' mechanism whereby a, ligand-induced conformational transition repositions the amphipathic, alpha-helix of the AF-2 activating domain and forms a transcriptionally, active receptor.

The 2.0-A crystal structure of the ligand-binding domain (LBD) of the human retinoic acid receptor (RAR)-gamma bound to all-trans retinoic acid reveals the ligand-binding interactions and suggests an electrostatic guidance mechanism. The overall fold is similar to that of the human RXR-alpha apo-LBD, except for the carboxy-terminal part which folds back towards the LBD core, contributing to the hydrophobic ligand pocket and 'sealing' its entry site. We propose a 'mouse trap' mechanism whereby a ligand-induced conformational transition repositions the amphipathic alpha-helix of the AF-2 activating domain and forms a transcriptionally active receptor.

==About this Structure==

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[[Category: Single protein]]

[[Category: Moras, D.]]

[[Category: Renaud, J.P.]]

[[Category: Renaud, J P.]]

[[Category: Rochel, N.]]

[[Category: Ruff, M.]]

[[Category: SPINE, Structural.Proteomics.in.Europe.]]

[[Category: SPINE, Structural Proteomics in Europe.]]

[[Category: REA]]

[[Category: active conformation]]

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[[Category: transcription regulation]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The 2.0-A crystal structure of the ligand-binding domain (LBD) of the, human retinoic acid receptor (RAR)-gamma bound to all-trans retinoic acid, reveals the ligand-binding interactions and suggests an electrostatic, guidance mechanism. The overall fold is similar to that of the human, RXR-alpha apo-LBD, except for the carboxy-terminal part which folds back, towards the LBD core, contributing to the hydrophobic ligand pocket and, 'sealing' its entry site. We propose a 'mouse trap' mechanism whereby a, ligand-induced conformational transition repositions the amphipathic, alpha-helix of the AF-2 activating domain and forms a transcriptionally, active receptor.
+The 2.0-A crystal structure of the ligand-binding domain (LBD) of the human retinoic acid receptor (RAR)-gamma bound to all-trans retinoic acid reveals the ligand-binding interactions and suggests an electrostatic guidance mechanism. The overall fold is similar to that of the human RXR-alpha apo-LBD, except for the carboxy-terminal part which folds back towards the LBD core, contributing to the hydrophobic ligand pocket and 'sealing' its entry site. We propose a 'mouse trap' mechanism whereby a ligand-induced conformational transition repositions the amphipathic alpha-helix of the AF-2 activating domain and forms a transcriptionally active receptor.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Moras, D.]]
-[[Category: Renaud, J.P.]]
+[[Category: Renaud, J P.]]
 [[Category: Rochel, N.]]
 [[Category: Ruff, M.]]
-[[Category: SPINE, Structural.Proteomics.in.Europe.]]
+[[Category: SPINE, Structural Proteomics in Europe.]]
 [[Category: REA]]
 [[Category: active conformation]]
@@ Line 32: / Line 32: @@
 [[Category: transcription regulation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:37:32 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:06:59 2008''