This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2l9l

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

NMR Structure of the Mouse MFG-E8 C2 Domain

Structural highlights

2l9l is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MFGM_MOUSE Contributes to phagocytic removal of apoptotic cells in many tissues. Specific ligand for the alpha-v/beta-3 and alpha-v/beta-5 receptors. Also binds to phosphatidylserine-enriched cell surfaces in a receptor-independent manner. Zona pellucida-binding protein which may play a role in gamete interaction (By similarity). Plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. Promotes VEGF-dependent neovascularization.^[1] ^[2]

Publication Abstract from PubMed

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.

NMR solution structure of C2 domain of MFG-E8 and insights into its molecular recognition with phosphatidylserine.,Ye H, Li B, Subramanian V, Choi BH, Liang Y, Harikishore A, Chakraborty G, Baek K, Yoon HS Biochim Biophys Acta. 2013 Mar;1828(3):1083-93. doi:, 10.1016/j.bbamem.2012.12.009. Epub 2012 Dec 21. PMID:23262193^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Silvestre JS, Thery C, Hamard G, Boddaert J, Aguilar B, Delcayre A, Houbron C, Tamarat R, Blanc-Brude O, Heeneman S, Clergue M, Duriez M, Merval R, Levy B, Tedgui A, Amigorena S, Mallat Z. Lactadherin promotes VEGF-dependent neovascularization. Nat Med. 2005 May;11(5):499-506. Epub 2005 Apr 17. PMID:15834428 doi:http://dx.doi.org/10.1038/nm1233
↑ Bu HF, Zuo XL, Wang X, Ensslin MA, Koti V, Hsueh W, Raymond AS, Shur BD, Tan XD. Milk fat globule-EGF factor 8/lactadherin plays a crucial role in maintenance and repair of murine intestinal epithelium. J Clin Invest. 2007 Dec;117(12):3673-83. PMID:18008006 doi:http://dx.doi.org/10.1172/JCI31841
↑ Ye H, Li B, Subramanian V, Choi BH, Liang Y, Harikishore A, Chakraborty G, Baek K, Yoon HS. NMR solution structure of C2 domain of MFG-E8 and insights into its molecular recognition with phosphatidylserine. Biochim Biophys Acta. 2013 Mar;1828(3):1083-93. doi:, 10.1016/j.bbamem.2012.12.009. Epub 2012 Dec 21. PMID:23262193 doi:http://dx.doi.org/10.1016/j.bbamem.2012.12.009

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2l9l"

Categories: Large Structures | Mus musculus | Ye H | Yoon HS

@@ Line 1: / Line 1: @@
 ==NMR Structure of the Mouse MFG-E8 C2 Domain==
-<StructureSection load='2l9l' size='340' side='right' caption='[[2l9l]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2l9l' size='340' side='right'caption='[[2l9l]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2l9l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L9L FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2l9l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L9L FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mfge8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2l9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9l OCA], [https://pdbe.org/2l9l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l9l RCSB], [https://www.ebi.ac.uk/pdbsum/2l9l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l9l ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9l OCA], [http://pdbe.org/2l9l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l9l RCSB], [http://www.ebi.ac.uk/pdbsum/2l9l PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MFGM_MOUSE MFGM_MOUSE]] Contributes to phagocytic removal of apoptotic cells in many tissues. Specific ligand for the alpha-v/beta-3 and alpha-v/beta-5 receptors. Also binds to phosphatidylserine-enriched cell surfaces in a receptor-independent manner. Zona pellucida-binding protein which may play a role in gamete interaction (By similarity). Plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. Promotes VEGF-dependent neovascularization.<ref>PMID:15834428</ref> <ref>PMID:18008006</ref>
+[https://www.uniprot.org/uniprot/MFGM_MOUSE MFGM_MOUSE] Contributes to phagocytic removal of apoptotic cells in many tissues. Specific ligand for the alpha-v/beta-3 and alpha-v/beta-5 receptors. Also binds to phosphatidylserine-enriched cell surfaces in a receptor-independent manner. Zona pellucida-binding protein which may play a role in gamete interaction (By similarity). Plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. Promotes VEGF-dependent neovascularization.<ref>PMID:15834428</ref> <ref>PMID:18008006</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 21: @@
 __TOC__
 </StructureSection>
-[[Category: Lk3 transgenic mice]]
+[[Category: Large Structures]]
-[[Category: Ye, H]]
+[[Category: Mus musculus]]
-[[Category: Yoon, H S]]
+[[Category: Ye H]]
-[[Category: Apoptosis]]
+[[Category: Yoon HS]]
-[[Category: Phosphatidylserine-binding protein]]

2l9l

From Proteopedia

Current revision

NMR Structure of the Mouse MFG-E8 C2 Domain

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox