Gohlke U, Gomis-Rüth F X, Crabbe T, Murphy G, Docherty A J, Bode W
Max-Planck-Institut für Biochemie, Abteilung für Strukturforschung, Martinsried bei München, Germany.
FEBS Lett. 1996 Jan 8;378(2):126-30. doi: 10.1016/0014-5793(95)01435-7.
In common with most other matrix metalloproteinases, gelatinase A has a non-catalytic C-terminal domain that displays sequence homology to haemopexin. Crystals of this domain were used by molecular replacement to solve its molecular structure at 2.6 A resolution, which was refined to an R value of 17.9%. This structure has a disc-like shape, with the chain folded into a beta-propeller structure that has pseudo four-fold symmetry. Although the topology and the side-chain arrangement are very similar to the equivalent domain of fibroblast collagenase, significant differences in surface charge and contouring are observable on 1 side of the gelatinase A disc. This difference might be a factor in allowing the gelatinase A C-terminal domain to bind to natural inhibitor TIMP-2.
与大多数其他基质金属蛋白酶一样，明胶酶A具有一个非催化性的C末端结构域，该结构域与血红素结合蛋白具有序列同源性。利用该结构域的晶体通过分子置换法以2.6埃的分辨率解析了其分子结构，最终精修至R值为17.9%。该结构呈盘状，链折叠成具有假四重对称性的β-螺旋桨结构。尽管其拓扑结构和侧链排列与成纤维细胞胶原酶的等效结构域非常相似，但在明胶酶A盘的一侧可观察到表面电荷和轮廓的显著差异。这种差异可能是明胶酶A的C末端结构域能够与天然抑制剂TIMP-2结合的一个因素。
