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![[Figure 6]](jb5026fig6mag.jpg)
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Figure 6
Ribbon models of domains of β-barrels containing β-links. Barrels are coloured gold, β-links are coloured red and the polypeptide chain between the β-turn of the β-link and the connecting β-strand is coloured purple. (a) Four-stranded, partly open, β-barrel: α-spectrin (PDB entry 1bk2; Martinez et al., 1998  ): SCOPe domain d1bk2a_, family b.34.2.1. (i) View from the side of the barrel. (ii) View from the `top' of the barrel. (b) Four-stranded, partly open, β-barrel: PDZ domain of human pick1 (PDB entry 2gzv; Elkins et al., 2007): SCOPe domain d2gzva1, family b.36.1.0. (i) Ribbon representation. (ii) Backbone detail with the β-link coloured CPK and adjacent parts of the strands coloured salmon pink. The arrowhead indicates the position of the single flanking hydrogen bond. (c) Six-stranded, closed, β-barrel: ferredoxin reductase (PDB entry 1fnc; Bruns & Karplus, 1995): SCOPe domain d1fnca1, family b.43.4.2. (d) Double-ψ, closed, six-stranded β-barrel: endogluconase V (PDB entry 2eng; Davies et al., 1995): SCOPe domain d2eng_, family b.52.1.1, with two β-links. (e) Eight-stranded, closed β-barrel: cyclophilin (PDB entry 2cpl; Ke, 1992): SCOPe domain d2cpla_, SCOPe family b.62.1.1. It has two β-links; the nonstandard one is marked with an arrowhead. |
![[Figure 6]](jb5026fig6.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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