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Conformational states of the glucocorticoid receptor DNA-binding domain from molecular dynamics simulations
Södertörns högskola, Avdelning Naturvetenskap. Karolinska Institutet.
Karolinska Institutet.
2002 (engelsk)Inngår i: Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, E-ISSN 1097-0134, Vol. 49, nr 1, s. 24-36Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Molecular dynamics simulations (MD) have been performed on variant crystal and NMR-derived structures of the glucocorticoid receptor DNA-binding domain (GR DBD). A loop region five residues long, the so-called D-box, exhibits significant flexibility, and transient perturbations of the tetrahedral geometry of two structurally important Cys4 zinc finger are seen, coupled to conformational changes in the D-box. In some cases, one of the Cys ligands to zinc exchanges with water, although no global distortion of the protein structure is observed. Thus, from MD simulation, dynamics of the D-box could partly be explained by solvent effects in conjunction with structural reformation of the zinc finger.

sted, utgiver, år, opplag, sider
2002. Vol. 49, nr 1, s. 24-36
Emneord [en]
zinc finger, nuclear receptors, DNA-binding domain, conformational change, molecular dynamics
HSV kategori
Identifikatorer
URN: urn:nbn:se:sh:diva-15826DOI: 10.1002/prot.10195ISI: 000177797300004PubMedID: 12211013Scopus ID: 2-s2.0-0036783390OAI: oai:DiVA.org:sh-15826DiVA, id: diva2:508344
Tilgjengelig fra: 2012-03-08 Laget: 2012-03-08 Sist oppdatert: 2018-01-26bibliografisk kontrollert

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