4wo1

From Proteopedia

Crystal structure of the DAP12 transmembrane domain in lipid cubic phase

PDB ID 4wo1

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Structural highlights

4wo1 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.14Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

TYOBP_HUMAN Nasu-Hakola disease. The disease is caused by mutations affecting the gene represented in this entry.

Function

TYOBP_HUMAN Non-covalently associates with activating receptors of the CD300 family. Cross-linking of CD300-TYROBP complexes results in cellular activation. Involved for instance in neutrophil activation mediated by integrin.

Publication Abstract from PubMed

The membrane-spanning alpha helices of single-pass receptors play crucial roles in stabilizing oligomeric structures and transducing biochemical signals across the membrane. Probing intermolecular transmembrane interactions in single-pass receptors presents unique challenges, reflected in a gross underrepresentation of their membrane-embedded domains in structural databases. Here, we present two high-resolution structures of transmembrane assemblies from a eukaryotic single-pass protein crystallized in a lipidic membrane environment. Trimeric and tetrameric structures of the immunoreceptor signaling module DAP12, determined to 1.77-A and 2.14-A resolution, respectively, are organized by the same polar surfaces that govern intramembrane assembly with client receptors. We demonstrate that, in addition to the well-studied dimeric form, these trimeric and tetrameric structures are made in cells, and their formation is competitive with receptor association in the ER. The polar transmembrane sequences therefore act as primary determinants of oligomerization specificity through interplay between charge shielding and sequestration of polar surfaces within helix interfaces.

Transmembrane Complexes of DAP12 Crystallized in Lipid Membranes Provide Insights into Control of Oligomerization in Immunoreceptor Assembly.,Knoblich K, Park S, Lutfi M, van 't Hag L, Conn CE, Seabrook SA, Newman J, Czabotar PE, Im W, Call ME, Call MJ Cell Rep. 2015 May 26;11(8):1184-92. doi: 10.1016/j.celrep.2015.04.045. Epub 2015, May 14. PMID:25981043^[1]

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

References

↑ Knoblich K, Park S, Lutfi M, van 't Hag L, Conn CE, Seabrook SA, Newman J, Czabotar PE, Im W, Call ME, Call MJ. Transmembrane Complexes of DAP12 Crystallized in Lipid Membranes Provide Insights into Control of Oligomerization in Immunoreceptor Assembly. Cell Rep. 2015 May 26;11(8):1184-92. doi: 10.1016/j.celrep.2015.04.045. Epub 2015, May 14. PMID:25981043 doi:http://dx.doi.org/10.1016/j.celrep.2015.04.045