PDBsum entry 3j82

Membrane protein/adp-binding protein

PDB id: 3j82

Contents

Protein chains

131 a.a.

374 a.a.

Ligands

ADP ×3

Metals

_CA

PDB id:

3j82

Name:

Membrane protein/adp-binding protein

Title:

Electron cryo-microscopy of dngr-1 in complex with f-actin

Structure:

C-type lectin domain family 9 member a. Chain: a. Synonym: dendritic cell natural killer lectin group receptor 1. Engineered: yes. Actin, cytoplasmic 1. Chain: b, c, d. Synonym: beta-actin, actin, cytoplasmic 1, n-terminally processed

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: clec9a, dngr-1. Expressed in: homo sapiens. Expression_system_taxid: 9606. Homo sapiens. Human. Organism_taxid: 9606.

Authors:

P.Hanc,T.Fujii,Y.Yamada,J.Huotari,O.Schulz,S.Ahrens,S.Kjaer,M.Way, K.Namba,C.Reis E Sousa

Key ref:

P.Hanč et al. (2015). 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. Immunity, 42, 839-849. PubMed id: 25979418 DOI: 10.1016/j.immuni.2015.04.009

Date:

25-Sep-14 Release date: 20-May-15

Protein chain

Q8BRU4  (CLC9A_MOUSE) -  C-type lectin domain family 9 member A from Mus musculus

Seq: 238 a.a.

Struc: 131 a.a.

Protein chains

P60709  (ACTB_HUMAN) -  Actin, cytoplasmic 1 from Homo sapiens

Seq: 375 a.a.

Struc: 374 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: Chains B, C, D: E.C.3.6.4.- - ?????

DOI no: 10.1016/j.immuni.2015.04.009

Immunity 42:839-849 (2015)

PubMed id: 25979418

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.

P.Hanč, T.Fujii, S.Iborra, Y.Yamada, J.Huotari, O.Schulz, S.Ahrens, S.Kjær, M.Way, D.Sancho, K.Namba, C.Reis e Sousa.

ABSTRACT

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 Å 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.