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3uaf

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Revision as of 02:32, 25 December 2014

Crystal Structure of a TTR-52 mutant of C. elegans

Structural highlights

3uaf is a 1 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[G5ED35_CAEEL] Plays a role as a bridging molecule that mediates recognition and engulfment of apoptotic cells by cross-linking the surface-exposed phosphatidylserine with the extracellular domain of the phagocyte receptor ced-1. Important for the generation of extracellular phosphatidylserine vesicles that promote loss of the exoplasmic leaflet from apoptotic cells in a time-dependent manner. Required for the exposure of exoplasmic leaflet on the phagocytic cells surrounding the apoptotic cells. Does not affect the phosphatidylserine externalization in living cells. May play a role in mediating transfer of phosphatidylserine from phosphatidylserine vesicles to ced-1 bearing phagocytes or alternatively result in the activation of a phosphatidylserine transporter in the phagocyte that promotes phosphatidylserine externalization.^[1] ^[2] ^[3]

Publication Abstract from PubMed

During apoptosis, apoptotic cells are removed by professional phagocytes or neighboring engulfing cells either directly through phagocytic receptors or indirectly through bridging molecules that cross-link dying cells to phagocytes. However, how bridging molecules recognize "eat me" signals and phagocytic receptors to mediate engulfment remains unclear. Here, we report the structural and functional studies of Caenorhabditis elegans TTR-52, a recently identified bridging molecule that cross-links surface-exposed phosphatidylserine (PtdSer) on apoptotic cells to the CED-1 receptor on phagocytes. Crystal structure studies show that TTR-52 has an open beta-barrel-like structure with some similarities to the PKCalpha-C2 domain. TTR-52 is proposed to bind PtdSer via an "ion-mediating" PtdSer-binding mode. Intensive functional studies show that CED-1 binds TTR-52 through its N-terminal EMI domain and that the hydrophobic region of the TTR-52 C terminus is involved in this interaction. In addition, unlike other PtdSer-binding domains, TTR-52 forms dimers, and its dimerization is important for its function in vivo. Our results reveal the first full-length structure of a bridging molecule and the mechanism underlying bridging molecule-mediated apoptotic cell recognition.

Structural study of TTR-52 reveals the mechanism by which a bridging molecule mediates apoptotic cell engulfment.,Kang Y, Zhao D, Liang H, Liu B, Zhang Y, Liu Q, Wang X, Liu Y Genes Dev. 2012 Jun 15;26(12):1339-50. PMID:22713871^[4]

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

References

↑ Wang X, Li W, Zhao D, Liu B, Shi Y, Chen B, Yang H, Guo P, Geng X, Shang Z, Peden E, Kage-Nakadai E, Mitani S, Xue D. Caenorhabditis elegans transthyretin-like protein TTR-52 mediates recognition of apoptotic cells by the CED-1 phagocyte receptor. Nat Cell Biol. 2010 Jul;12(7):655-64. doi: 10.1038/ncb2068. Epub 2010 Jun 6. PMID:20526330 doi:http://dx.doi.org/10.1038/ncb2068
↑ Zhang Y, Wang H, Kage-Nakadai E, Mitani S, Wang X. C. elegans secreted lipid-binding protein NRF-5 mediates PS appearance on phagocytes for cell corpse engulfment. Curr Biol. 2012 Jul 24;22(14):1276-84. doi: 10.1016/j.cub.2012.06.004. Epub 2012 , Jun 21. PMID:22727700 doi:http://dx.doi.org/10.1016/j.cub.2012.06.004
↑ Mapes J, Chen YZ, Kim A, Mitani S, Kang BH, Xue D. CED-1, CED-7, and TTR-52 regulate surface phosphatidylserine expression on apoptotic and phagocytic cells. Curr Biol. 2012 Jul 24;22(14):1267-75. doi: 10.1016/j.cub.2012.05.052. Epub 2012 , Jun 21. PMID:22727702 doi:http://dx.doi.org/10.1016/j.cub.2012.05.052
↑ Kang Y, Zhao D, Liang H, Liu B, Zhang Y, Liu Q, Wang X, Liu Y. Structural study of TTR-52 reveals the mechanism by which a bridging molecule mediates apoptotic cell engulfment. Genes Dev. 2012 Jun 15;26(12):1339-50. PMID:22713871 doi:http://dx.doi.org/10.1101/gad.187815.112

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/3uaf"

@@ Line 5: / Line 5: @@
 </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=3uaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uaf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3uaf RCSB], [http://www.ebi.ac.uk/pdbsum/3uaf PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/G5ED35_CAEEL G5ED35_CAEEL]] Plays a role as a bridging molecule that mediates recognition and engulfment of apoptotic cells by cross-linking the surface-exposed phosphatidylserine with the extracellular domain of the phagocyte receptor ced-1. Important for the generation of extracellular phosphatidylserine vesicles that promote loss of the exoplasmic leaflet from apoptotic cells in a time-dependent manner. Required for the exposure of exoplasmic leaflet on the phagocytic cells surrounding the apoptotic cells. Does not affect the phosphatidylserine externalization in living cells. May play a role in mediating transfer of phosphatidylserine from phosphatidylserine vesicles to ced-1 bearing phagocytes or alternatively result in the activation of a phosphatidylserine transporter in the phagocyte that promotes phosphatidylserine externalization.<ref>PMID:20526330</ref> <ref>PMID:22727700</ref> <ref>PMID:22727702</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

3uaf

From Proteopedia

Revision as of 02:32, 25 December 2014

Crystal Structure of a TTR-52 mutant of C. elegans

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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