Structural highlights
Function
MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
Publication Abstract from PubMed
NLRP12 is a NOD-like receptor that plays multiple roles in both inflammation and tumorigenesis. Despite the importance, little is known about its mechanism of action at the molecular level. Here, we report the crystal structure of NLRP12 PYD domain at 1.70 A fused with an maltose-binding protein (MBP) tag. Interestingly, the PYD domain forms a dimeric configuration through a disulfide bond in the crystal. The possible biological significance is discussed in the context of ROS induced NF-kappaB activation.
Crystal structure of human NLRP12 PYD domain and implication in homotypic interaction.,Jin T, Huang M, Jiang J, Smith P, Xiao TS PLoS One. 2018 Jan 2;13(1):e0190547. doi: 10.1371/journal.pone.0190547. , eCollection 2018. PMID:29293680[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jin T, Huang M, Jiang J, Smith P, Xiao TS. Crystal structure of human NLRP12 PYD domain and implication in homotypic interaction. PLoS One. 2018 Jan 2;13(1):e0190547. PMID:29293680 doi:10.1371/journal.pone.0190547
