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Cover Illustration: The envelope of the human respiratory syncytial virus contains a small hydrophobic (SH) protein, 64 amino acids long, with one α-helical transmembrane domain. A combination of structural and functional studies provide evidence that this transmembrane domain forms a homopentameric α-helical bundle with cation-selective ion channel activity. This figure shows consecutive slices through this pentameric model, from residue Leu20 to Asn42. The color code is as follows: Ile, green; Leu, salmon; Thr, marine; Ser, cyan; Met, orange; His, red; Ala, yellow; Asn, blue. All polar residues are oriented either toward the helix–helix interface, or toward the lumen of the pore, suggesting involvement in pentamer stabilization or channel selectivity. (For details, see Gan et al., pp. 813–820.)