ORTHOGONAL PACKING OF BETA-PLEATED SHEETS IN PROTEINS
ORTHOGONAL PACKING OF BETA-PLEATED SHEETS IN PROTEINS
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DOI:
10.1021/bi00260a009
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发表时间:
1982-01-01
期刊:
影响因子:
2.9
通讯作者:
JANIN, J
中科院分区:
文献类型:
--
作者:
CHOTHIA, C;JANIN, J
Two classes of .beta.-sheet to .beta.-sheet packing can be distinguished in globular proteins. Both classes have .beta. sheets with the usual right-handed twist packed face to face. In orthogonal .beta.-sheet packings, the strand directions of the different .beta. sheets are 90.degree. to each other. Twisted .beta. sheets in this orientation have anticomplementary surfaces: one pair of diagonally opposite corners in the .beta. sheets are very close, and the other pairs of corners splay apart. At the close corners, the .beta. sheets are usually covalently connected: a strand that is part of one .beta. sheet turns through a right-handed bend to become part of the second .beta. sheet. The bend may occur at a .beta. bulge, or over a stretch of residues with a characteristic conformation, forming a .beta. bend. Contacts between the .beta. sheets occur along the diagonal joining the close corners. They involve about one-fourth of the .beta.-sheet residues, and two-thirds of them are Val, Ile, or Leu. Elsewhere, the space between the .beta. sheets is filled by side chains from other parts of the protein, often .alpha. helices placed at the splayed corners. Examples of orthogonal .beta.-sheet packing are found in alcohol dehydrogenase, the acid proteases, the trypsin family, papain, staphylococcal nuclease, and thermolysin. In aligned .beta.-sheet packings, the angle between the strand directions of the packed .beta. sheets is .apprx. 30.degree.. In this orientation, the twisted .beta.-sheet surfaces are complementary. The principles governing this class of .beta.-sheet packings were described previously. The differences and similarities of the aligned and orthogonal packing classes are discussed.