Next Article in Journal
Diarylheptanoid Glycosides of Morella salicifolia Bark
Previous Article in Journal
Vanadium Compounds as PTP Inhibitors
Open AccessArticle

Domain IV of Annexin A5 Is Critical for Binding Calcium and Guarantees Its Maximum Binding to the Phosphatidylserine Membrane

by Jie Wang 1, Jing Liu 1, Yulu Cao 2, Minjin Hu 2 and Zichun Hua 1,3,*
1
State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing University, Nanjing 210023, China
2
Jiangsu TargetPharma Laboratories Inc., Changzhou High-Tech Research Institute of Nanjing University, Changzhou 213164, China
3
Shenzhen Research Institute of Nanjing University, Shenzhen 518057, China
*
Author to whom correspondence should be addressed.
Molecules 2017, 22(12), 2256; https://doi.org/10.3390/molecules22122256
Received: 21 November 2017 / Revised: 8 December 2017 / Accepted: 14 December 2017 / Published: 19 December 2017
Background: Although domain IV of annexin A5 (anxA5) may be less effective in binding phosphatidylserine (PS), the four domains together may guarantee the maximum binding of anxA5 to the PS membrane. Additionally, previous research has shown that annexin mutants lacking one or more domain(s) have different biological activities compared to the wild-type. The present research mainly aims to study the role of domain IV in the crucial PS-binding function of anxA5. Methods: The domain IV-truncated anxA5 protein was constructed and purified. Isothermal titration calorimetry, flow cytometry and activated partial thromboplastin time were adopted to examine the function of domain IV in anxA5-PS binding directly or indirectly. Results: The domain IV-truncated form of anxA5 is impaired in binding PS liposome and apoptotic cells, and anticoagulation activity. The mutant cannot bind calcium, but binds PS only in the presence of calcium. Conclusions: Truncation of domain IV of anxA5 destroys its calcium-binding ability and impairs its PS-binding activity. Truncation of domain IV may induce conformation change of anxA5 or reduce the hydrophobic interactions between protein and membrane, which may explain the decrease of PS-binding affinity of the mutant. View Full-Text
Keywords: annexin A5; domain IV; calcium; phosphatidylserine; binding annexin A5; domain IV; calcium; phosphatidylserine; binding
Show Figures

Figure 1

MDPI and ACS Style

Wang, J.; Liu, J.; Cao, Y.; Hu, M.; Hua, Z. Domain IV of Annexin A5 Is Critical for Binding Calcium and Guarantees Its Maximum Binding to the Phosphatidylserine Membrane. Molecules 2017, 22, 2256.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop