Crystal structure of calcium bound domain VI of calpain at 1.9 Å resolution and its role in enzyme assembly, regulation, and inhibitor binding
Crystal structure of calcium bound domain VI of calpain at 1.9 Å resolution and its role in enzyme assembly, regulation, and inhibitor binding
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1.9 Å 分辨率下钙蛋白酶钙结合域 VI 的晶体结构及其在酶组装、调节和抑制剂结合中的作用
DOI:
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发表时间:
1997
期刊:
影响因子:
--
通讯作者:
S. Narayana
中科院分区:
文献类型:
--
作者:
G. Lin;D. Chattopadhyay;M. Maki;K. Wang;M. Carson;Lei Jin;P. Yuen;E. Takano;M. Hatanaka;L. DeLucas;S. Narayana
The three dimensional structure of calcium-bound domain VI of porcine calpain has been determined to 1.9 Å resolution. The crystal structure reveals five EF-hands, one more than previously suggested. There are two EF-hand pairs, one pair (EF1-EF2) displays an ‘open’ conformation and the other (EF3-EF4) a ‘closed’ conformation. Unusually, a calcium atom is found at the C-terminal end of the calcium binding loop of EF4. With two additional residues in the calcium binding loop, the fifth EF-hand (EF5) is in a ‘closed’ conformation. EF5 pairs up with the corresponding fifth EF-hand of a non-crystallographically related molecule. Considering the EFS's role in a homodimer formation of domain VI, we suggest a model for the assembly of heterodimeric calpain. The crystal structure of a Ca2+ bound domain VI–inhibitor (PD150606) complex has been refined to 2.1 Å resolution. A possible mode for calpain inhibition is discussed.
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影响因子:
3.1
作者:
Zhang,W;Mellgren,RL
通讯作者:
Mellgren,RL
DOI:
10.1073/pnas.88.16.7233
发表时间:
1991-08-01
影响因子:
11.1
作者:
LEE, KS;FRANK, S;LYNCH, G
通讯作者:
LYNCH, G
影响因子:
10.8
作者:
Anggrahini, Dyah W.;Emoto, Noriaki;Hirata, Ken-ichi
通讯作者:
Hirata, Ken-ichi
影响因子:
2.9
作者:
COOK, WJ;WALTER, LJ;WALTER, MR
通讯作者:
WALTER, MR
DOI:
10.1016/0167-4838(88)90066-0
发表时间:
1988
期刊:
Biochimica et biophysica acta
影响因子:
--
作者:
Mellgren,RL;Lane,RD
通讯作者:
Lane,RD