2L9L
NMR Structure of the Mouse MFG-E8 C2 Domain
Summary for 2L9L
| Entry DOI | 10.2210/pdb2l9l/pdb |
| NMR Information | BMRB: 17477 |
| Descriptor | Lactadherin (1 entity in total) |
| Functional Keywords | apoptosis, phosphatidylserine-binding protein |
| Biological source | Mus musculus (mouse) |
| Cellular location | Membrane; Peripheral membrane protein: P21956 |
| Total number of polymer chains | 1 |
| Total formula weight | 19437.76 |
| Authors | Ye, H.,Yoon, H.S. (deposition date: 2011-02-21, release date: 2012-08-29, Last modification date: 2024-10-30) |
| Primary citation | Ye, H.,Li, B.,Subramanian, V.,Choi, B.H.,Liang, Y.,Harikishore, A.,Chakraborty, G.,Baek, K.,Yoon, H.S. NMR solution structure of C2 domain of MFG-E8 and insights into its molecular recognition with phosphatidylserine Biochim.Biophys.Acta, 1828:1083-1093, 2013 Cited by PubMed Abstract: 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 phosphatidylcholine (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, and characterized the molecular basis of binding between the C2 domain and PS by (31)P-NMR spectroscopy. Furthermore, we also verified that that positively charged and aromatic residues clustered in loops 1-3 of the C2 domain play key roles in recognizing PS in apoptotic cells. PubMed: 23262193DOI: 10.1016/j.bbamem.2012.12.009 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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