7wf9

Crystal structure of mouse SNX25 RGS domain in space group P41212

spinqualitylabelsall models 7wf9, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7wf9 is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.55Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SNX25_MOUSE May be involved in several stages of intracellular trafficking. Publication Abstract from PubMed As a subgroup of sorting nexins (SNXs) that contain regulator of G protein signaling homology (RH) domain, SNX-RH proteins, including SNX13, SNX14 and SNX25, were proposed to play bifunctional roles in protein sorting and GPCR signaling regulation. However, mechanistic details of SNX-RH proteins functioning via RH domain remain to be illustrated. Here, we delineate crystal structures of the RH domains of SNX13 and SNX25, revealing a homodimer of SNX13 RH domain mediated by unique extended alpha4 and alpha5 helices, and a thiol modulated homodimer of SNX25-RH triggered by a unique cysteine on alpha6 helix. Further studies showed that RH domains of SNX-RH do not possess binding capacity toward Galpha subunits, owing to the lack of critical residues for interaction. Thus, this study identifies a group of novel non-canonical RH domains that can act as a dimerization module in sorting nexins, which provides structural basis for mechanism studies on SNX-RH protein functions. Structural Studies Reveal Unique Non-canonical Regulators of G Protein Signaling Homology (RH) Domains in Sorting Nexins.,Zhang Y, Chen R, Dong Y, Zhu J, Su K, Liu J, Xu J J Mol Biol. 2022 Nov 15;434(21):167823. doi: 10.1016/j.jmb.2022.167823. Epub 2022 , Sep 11. PMID:36103920 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Sorting nexin 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA