3j82
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Electron cryo-microscopy of DNGR-1 in complex with F-actin== | ==Electron cryo-microscopy of DNGR-1 in complex with F-actin== | ||
| - | <StructureSection load='3j82' size='340' side='right' caption='[[3j82]], [[Resolution|resolution]] 7.70Å' scene=''> | + | <StructureSection load='3j82' size='340' side='right'caption='[[3j82]], [[Resolution|resolution]] 7.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3j82]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J82 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J82 FirstGlance]. <br> | <table><tr><td colspan='2'>[[3j82]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J82 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J82 FirstGlance]. <br> | ||
| Line 13: | Line 13: | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/CLC9A_MOUSE CLC9A_MOUSE]] Functions as an endocytic receptor on a small subset of myeloid cells specialized for the uptake and processing of material from dead cells. Recognizes filamentous form of actin in association with particular actin-binding domains of cytoskeletal proteins, including spectrin, exposed when cell membranes are damaged, and mediate the cross-presentation of dead-cell associated antigens in a Syk-dependent manner.<ref>PMID:18408006</ref> <ref>PMID:18497879</ref> <ref>PMID:19219027</ref> <ref>PMID:22483802</ref> [[http://www.uniprot.org/uniprot/ACTB_HUMAN ACTB_HUMAN]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. | [[http://www.uniprot.org/uniprot/CLC9A_MOUSE CLC9A_MOUSE]] Functions as an endocytic receptor on a small subset of myeloid cells specialized for the uptake and processing of material from dead cells. Recognizes filamentous form of actin in association with particular actin-binding domains of cytoskeletal proteins, including spectrin, exposed when cell membranes are damaged, and mediate the cross-presentation of dead-cell associated antigens in a Syk-dependent manner.<ref>PMID:18408006</ref> <ref>PMID:18497879</ref> <ref>PMID:19219027</ref> <ref>PMID:22483802</ref> [[http://www.uniprot.org/uniprot/ACTB_HUMAN ACTB_HUMAN]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | DNGR-1 is a C-type lectin receptor that binds F-actin exposed by dying cells and facilitates cross-presentation of dead cell-associated antigens by dendritic cells. Here we present the structure of DNGR-1 bound to F-actin at 7.7 A resolution. Unusually for F-actin binding proteins, the DNGR-1 ligand binding domain contacts three actin subunits helically arranged in the actin filament, bridging over two protofilaments, as well as two neighboring actin subunits along one protofilament. Mutation of residues predicted to mediate ligand binding led to loss of DNGR-1-dependent cross-presentation of dead cell-associated antigens, formally demonstrating that the latter depends on F-actin recognition. Notably, DNGR-1 has relatively modest affinity for F-actin but multivalent interactions allow a marked increase in binding strength. Our findings shed light on modes of actin binding by cellular proteins and reveal how extracellular detection of cytoskeletal components by dedicated receptors allows immune monitoring of loss of cellular integrity. | ||
| + | |||
| + | Structure of the Complex of F-Actin and DNGR-1, a C-Type Lectin Receptor Involved in Dendritic Cell Cross-Presentation of Dead Cell-Associated Antigens.,Hanc P, Fujii T, Iborra S, Yamada Y, Huotari J, Schulz O, Ahrens S, Kjaer S, Way M, Sancho D, Namba K, Reis e Sousa C Immunity. 2015 May 19;42(5):839-849. doi: 10.1016/j.immuni.2015.04.009. Epub 2015, May 12. PMID:25979418<ref>PMID:25979418</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3j82" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Actin|Actin]] | + | *[[Actin 3D structures|Actin 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
| Line 21: | Line 30: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Lk3 transgenic mice]] | [[Category: Lk3 transgenic mice]] | ||
[[Category: Ahrens, S]] | [[Category: Ahrens, S]] | ||
Revision as of 08:10, 18 December 2019
Electron cryo-microscopy of DNGR-1 in complex with F-actin
| |||||||||||
Categories: Homo sapiens | Large Structures | Lk3 transgenic mice | Ahrens, S | Fujii, T | Hanc, P | Huotari, J | Kjaer, S | Namba, K | Schulz, O | Sousa, C Reis e | Way, M | Yamada, Y | Actin | Dngr-1 | Membrane protein-adp-binding protein complex | Recognition of damage-associated molecular pattern
