NMR solution structure of C2 domain of MFG-E8 and insights into its recognition with phosphatidylserine
MFG-E8 (also known as lactadherin), which is a secreted glycoprotein from a variety of cell types, possesses two EGF domains and tandem C domains with sequence homology to that of blood coagulation proteins factor V and factor VIII. MFG-E8 binds to phosphatidylserine (PS) in membranes with high affi...
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sg-ntu-dr.10356-548552023-02-28T18:40:03Z NMR solution structure of C2 domain of MFG-E8 and insights into its recognition with phosphatidylserine Li, Baihong Yoon Ho Sup School of Biological Sciences DRNTU::Science::Biological sciences MFG-E8 (also known as lactadherin), which is a secreted glycoprotein from a variety of cell types, possesses two EGF domains and tandem C domains with sequence homology to that of blood coagulation proteins factor V and factor VIII. MFG-E8 binds to phosphatidylserine (PS) in membranes with high affinity. We have recently shown that the C2 domain of MFG-E8 bears more specificity toward PS when compared with phophatidylcholine (PC), another phospholipid thought to be involved in the immune function of phagocytes. In our current study, we have determined the solution structure of the C2 domain by nuclear magnetic resonance (NMR) spectroscopy, characterized the molecular basis of binding between the C2 domain and PS by 31P-NMR spectroscopy. Furthermore, we also verified that positively charged and aromatic residues clustered in loops 1-3 of the C2 domain play key roles in recognizing PS in apoptotic cells. Last but not least, the influence of C1 domain on PS binding was also tested in our new Co-culture FACS analysis and confirmed its role in the binding event. DOCTOR OF PHILOSOPHY (SBS) 2013-09-30T06:39:55Z 2013-09-30T06:39:55Z 2013 2013 Thesis Li,B. (2013). NMR solution structure of C2 domain of MFG-E8 and insights into its recognition with phosphatidylserine.. Doctoral thesis, Nanyang Technological University, Singapore. https://hdl.handle.net/10356/54855 10.32657/10356/54855 en 139 p. application/pdf |
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DRNTU::Science::Biological sciences Li, Baihong NMR solution structure of C2 domain of MFG-E8 and insights into its recognition with phosphatidylserine |
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MFG-E8 (also known as lactadherin), which is a secreted glycoprotein from a variety of cell types, possesses two EGF domains and tandem C domains with sequence homology to that of blood coagulation proteins factor V and factor VIII. MFG-E8 binds to phosphatidylserine (PS) in membranes with high affinity. We have recently shown that the C2 domain of MFG-E8 bears more specificity toward PS when compared with phophatidylcholine (PC), another phospholipid thought to be involved in the immune function of phagocytes. In our current study, we have determined the solution structure of the C2 domain by nuclear magnetic resonance (NMR) spectroscopy, characterized the molecular basis of binding between the C2 domain and PS by 31P-NMR spectroscopy. Furthermore, we also verified that positively charged and aromatic residues clustered in loops 1-3 of the C2 domain play key roles in recognizing PS in apoptotic cells. Last but not least, the influence of C1 domain on PS binding was also tested in our new Co-culture FACS analysis and confirmed its role in the binding event. |
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Yoon Ho Sup |
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Yoon Ho Sup Li, Baihong |
format |
Theses and Dissertations |
author |
Li, Baihong |
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Li, Baihong |
title |
NMR solution structure of C2 domain of MFG-E8 and insights into its recognition with phosphatidylserine |
title_short |
NMR solution structure of C2 domain of MFG-E8 and insights into its recognition with phosphatidylserine |
title_full |
NMR solution structure of C2 domain of MFG-E8 and insights into its recognition with phosphatidylserine |
title_fullStr |
NMR solution structure of C2 domain of MFG-E8 and insights into its recognition with phosphatidylserine |
title_full_unstemmed |
NMR solution structure of C2 domain of MFG-E8 and insights into its recognition with phosphatidylserine |
title_sort |
nmr solution structure of c2 domain of mfg-e8 and insights into its recognition with phosphatidylserine |
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2013 |
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https://hdl.handle.net/10356/54855 |
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