Title |
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Primary response of the sGC heme binding domain to the cleavage of the Fe-His bond
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Authors |
Huali Zhang1, Ming Lu1,
Yuebin Zhang1, Zhengqiang Li1, * | |
Affiliation |
1Key Laboratory for Molecular Enzymology and Engineering of the Ministry of Education (Jilin University), 130021 Changchun, Jilin (P.R.China)
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Fax |
86 431 88499261; * Corresponding author
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Article Type |
Hypothesis
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Date |
received February 29, 2008; revised March 24, 2008; accepted March 25, 2008; published April 11, 2008
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Abstract |
Soluble guanylate cyclase (sGC) is an important heme sensor protein. Regulation of the status of heme in the heme binding domain (or HNOX domain) by various gaseous activators can increase the catalytic efficiency of the cyclase domain. Several studies have demonstrated that the full activation of sGC is directly related to the cleavage of the Fe-His bond of the HNOX domain. To expand the primary response of the sGC HNOX domain to the cleavage event, a structural model of the sGC HNOX domain was constructed using homology modeling and the Fe-His bond was released at 6 ns of a 10-ns molecular dynamics simulation. An instant increment of Cα-RMSD over L2 (Loop2, residues 124-130) was found after the cleavage of the Fe-His bond, which was consistent with the principle component analysis (PCA). The energy analysis results suggest that the motions of L2 are energetic. Based on the results, energetic conformational transformation of L2 is identified as the primary response of the sGC HNOX domain to the cleavage of the Fe-His bond.
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Keywords |
soluble guanylate cyclase; information transmission; HNOX domain; homology modeling; molecular dynamics
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Citation |
Zhang et al., Bioinformation 2(7): 296-300 (2008)
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Edited by |
P. Kangueane
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ISSN |
0973-2063
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Publisher |
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License |
This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License. |