Luo X, Hofmann K
Bioinformatics & Gene Discovery Group, MEMOREC Stoffel GmbH, Stöckheimer, Weg 1, D-50829 Köln, Germany.
Trends Biochem Sci. 2001 Mar;26(3):147-8. doi: 10.1016/s0968-0004(00)01768-0.
The non-catalytic part of proteases frequently harbours domains responsible for regulation or targeting. Here, we describe a novel sequence motif conserved in proteins that belong to different protease superfamilies, the subtilases and Zn-containing metalloproteases. The structure of the transferrin receptor, a catalytically inactive member of the latter family, suggests that the protease-associated domain forms a lid structure that covers the active site. In addition to proteases, the domain is also found in two different families of plant vacuolar sorting receptors.
蛋白酶的非催化部分常常含有负责调控或靶向定位的结构域。在此，我们描述了一种在属于不同蛋白酶超家族（枯草杆菌蛋白酶和含锌金属蛋白酶）的蛋白质中保守的新型序列基序。转铁蛋白受体是后一家族中无催化活性的成员，其结构表明，与蛋白酶相关的结构域形成了一个覆盖活性位点的盖子结构。除了蛋白酶外，该结构域还存在于植物液泡分选受体的两个不同家族中。
