Gomis-Rüth F X, Gohlke U, Betz M, Knäuper V, Murphy G, López-Otín C, Bode W
Max-Planck-Institut für Biochemie, Abteilung für Strukturforschung, Planegg-Martinsreid, Germany.
J Mol Biol. 1996 Dec 6;264(3):556-66. doi: 10.1006/jmbi.1996.0661.
Collagenase-3 (MMP-13) is a matrix metalloproteinase involved in human breast cancer pathology and in arthritic processes. The crystal structure of its C-terminal haemopexin-like domain has been solved by molecular replacement and refined to an R-value of 0.195 using data to 2.7 A resolution. This structure reveals a disk-like shape. The chain is folded into a beta-propeller structure of pseudo 4-fold symmetry, with the four propeller blades arranged around a funnel-like tunnel. This central tunnel tube harbours four ions assigned as two calcium and two chloride ions. The C-terminal domain of collagenase-3 has a similar structure to the equivalent domain of gelatinase A and fibroblast collagenase 1; however, its detailed structure and surface charge pattern has a somewhat greater similarity to the latter, in agreement with the subgrouping of MMP-13 with the collagenase subfamily of MMPs. It is proposed that several small structural differences may act together to confer the characteristic binding and cleavage specificities of collagenases for triple-helical substrates, probably in co-operation with a fitting interdomain linker.
胶原酶-3（MMP-13）是一种基质金属蛋白酶，参与人类乳腺癌病理过程和关节炎进程。其C端血红素结合蛋白样结构域的晶体结构已通过分子置换法解析，并利用分辨率为2.7埃的数据精修至R值为0.195。该结构呈盘状。链折叠成具有伪四重对称性的β-螺旋桨结构，四个螺旋桨叶片围绕着一个漏斗状通道排列。这个中央通道管容纳四个离子，被确定为两个钙离子和两个氯离子。胶原酶-3的C端结构域与明胶酶A和成纤维细胞胶原酶1的相应结构域具有相似结构；然而，其详细结构和表面电荷模式与后者更为相似，这与MMP-13在基质金属蛋白酶胶原酶亚家族中的分组一致。有人提出，几个小的结构差异可能共同作用，赋予胶原酶对三螺旋底物的特征性结合和切割特异性，可能与合适的结构域间连接子协同作用。
