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Structure of the lutein-binding domain of human StARD3 at 1.74 Šresolution and model of a complex with lutein.
Horvath, Martin P; George, Evan W; Tran, Quang T; Baumgardner, Kody; Zharov, Gabe; Lee, Sarah; Sharifzadeh, Hassan; Shihab, Saeed; Mattinson, Ty; Li, Binxing; Bernstein, Paul S.
Afiliación
  • Horvath MP; Department of Biology, University of Utah, 257 S 1400 E, Salt Lake City, UT 84112, USA.
  • George EW; Department of Biology, University of Utah, 257 S 1400 E, Salt Lake City, UT 84112, USA.
  • Tran QT; Department of Biology, University of Utah, 257 S 1400 E, Salt Lake City, UT 84112, USA.
  • Baumgardner K; Department of Biology, University of Utah, 257 S 1400 E, Salt Lake City, UT 84112, USA.
  • Zharov G; Department of Biology, University of Utah, 257 S 1400 E, Salt Lake City, UT 84112, USA.
  • Lee S; Department of Biology, University of Utah, 257 S 1400 E, Salt Lake City, UT 84112, USA.
  • Sharifzadeh H; Department of Ophthalmology and Visual Sciences, Moran Eye Center, University of Utah School of Medicine, Salt Lake City, UT 84132, USA.
  • Shihab S; Department of Ophthalmology and Visual Sciences, Moran Eye Center, University of Utah School of Medicine, Salt Lake City, UT 84132, USA.
  • Mattinson T; Department of Ophthalmology and Visual Sciences, Moran Eye Center, University of Utah School of Medicine, Salt Lake City, UT 84132, USA.
  • Li B; Department of Ophthalmology and Visual Sciences, Moran Eye Center, University of Utah School of Medicine, Salt Lake City, UT 84132, USA.
  • Bernstein PS; Department of Ophthalmology and Visual Sciences, Moran Eye Center, University of Utah School of Medicine, Salt Lake City, UT 84132, USA.
Acta Crystallogr F Struct Biol Commun ; 72(Pt 8): 609-18, 2016 08.
Article en En | MEDLINE | ID: mdl-27487925
A crystal structure of the lutein-binding domain of human StARD3 (StAR-related lipid-transfer protein 3; also known as MLN64) has been refined to 1.74 Šresolution. A previous structure of the same protein determined to 2.2 Šresolution highlighted homology with StARD1 and shared cholesterol-binding character. StARD3 has since been recognized as a carotenoid-binding protein in the primate retina, where its biochemical function of binding lutein with specificity appears to be well suited to recruit this photoprotective molecule. The current and previous structures correspond closely to each other (r.m.s.d. of 0.25 Å), especially in terms of the helix-grip fold constructed around a solvent-filled cavity. Regions of interest were defined with alternate conformations in the current higher-resolution structure, including Arg351 found within the cavity and Ω1, a loop of four residues found just outside the cavity entrance. Models of the complex with lutein generated by rigid-body docking indicate that one of the ionone rings must protrude outside the cavity, and this insight has implications for molecular interactions with transport proteins and enzymes that act on lutein. Interestingly, models with the ℇ-ionone ring characteristic of lutein pointing towards the bottom of the cavity were associated with fewer steric clashes, suggesting that steric complementarity and ligand asymmetry may play a role in discriminating lutein from the other ocular carotenoids zeaxanthin and meso-zeaxanthin, which only have ß-ionone rings.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Luteína / Proteínas Portadoras / Norisoprenoides / Zeaxantinas / Proteínas de la Membrana Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Acta Crystallogr F Struct Biol Commun Año: 2016 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Luteína / Proteínas Portadoras / Norisoprenoides / Zeaxantinas / Proteínas de la Membrana Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Acta Crystallogr F Struct Biol Commun Año: 2016 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos