Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/94378
Type: Artigo de periódico
Title: Crystallization And Preliminary X-ray Diffraction Studies Of Isoform α1 Of The Human Thyroid Hormone Receptor Ligand-binding Domain
Author: Nunes F.M.
Aparicio R.
Santos M.A.M.
Portugal R.V.
Dias S.M.G.
Neves F.A.R.
Simeoni L.A.
Baxter J.D.
Webb P.
Polikarpov I.
Abstract: Thyroid hormone receptors (TR) play critical roles in virtually all tissues. The TR ligand-binding domain (LBD) participates in important activities, such as transcriptional activation and repression, through conformational changes induced by hormone binding. Two crystal forms of isoform α1 of the human thyroid hormone receptor LBD (hTRα1) in complex with the thyroid hormones T3 and Triac were obtained. The hTRα1-T3 complex was crystallized in a previously unobserved crystal form (space group P2 12121, a = 59.98, b = 80.80, c = 102.21 Å), with diffraction patterns extending to 1.90 Å resolution on a rotating-anode X-ray source, and in space group C2 (a = 117.54, b = 80.66, c = 62.55 Å, β = 121.04°), with data extending to 2.32 Å resolution. The hTRα1-Triac complex was also crystallized in the new space group P212121, with unit-cell parameters a = 60.01, b = 80.82, c = 102.39 Å its resolution limit extended to 2.20 Å on a home source. Phasing was carried out by the molecular-replacement method and structural refinement is currently in progress. The refined structures may provide insight into the design of new thyromimetics. © 2004 International Union of Crystallography.
Editor: 
Rights: aberto
Identifier DOI: 10.1107/S0907444904017858
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-16644373256&partnerID=40&md5=71bca0a695382303dbcb09a7780b5dc1
Date Issue: 2004
Appears in Collections:Unicamp - Artigos e Outros Documentos

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