The C‐terminal (haemopexin‐like) domain structure of human gelatinase A (MMP2): structural implications for its function
The C‐terminal (haemopexin‐like) domain structure of human gelatinase A (MMP2): structural implications for its function
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人明胶酶 A (MMP2) 的 C 末端（类血红素结合蛋白）结构域：对其功能的结构影响
DOI：
10.1016/0014-5793(95)01435-7
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发表时间：
1996
期刊：
影响因子：
3.5
通讯作者：
W. Bode
中科院分区：
文献类型：
--
作者：
U. Gohlke;F. Gomis‐Rüth;T. Crabbe;G. Murphy;A. Docherty;W. Bode
与大多数其他基质金属蛋白酶一样，明胶酶 A 具有非催化 C 末端结构域，与血红素结合蛋白显示序列同源性。该域的晶体通过分子置换以2.6 Å的分辨率解析其分子结构，并将其R值精修至17.9%。该结构呈圆盘状，链条折叠成具有伪四重对称性的β螺旋桨结构。尽管拓扑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着差异。这种差异可能是明胶酶 A C 末端结构域与天然抑制剂 TIMP-2 结合的一个因素。
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 Å resolution, which was refined to anRvalue of 17.9%. This structure has a disc‐like shape, with the chain folded into a β‐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.
DOI：
--
发表时间：
1993-07
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
A. Strongin;B. Marmer;G. A. Grant;G. Goldberg
通讯作者：
A. Strongin;B. Marmer;G. A. Grant;G. Goldberg
人 92-kDa IV 型胶原酶纤连蛋白样胶原结合域的丙氨酸扫描诱变和功能分析。
DOI：
--
发表时间：
1992
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Collier,IE;Krasnov,PA;Strongin,AY;Birkedal-Hansen,H;Goldberg,GI
通讯作者：
Goldberg,GI