7ur2

Crystal structure of the Sec14 domain of the RhoGEF Kalirin

spinqualitylabelsall models 7ur2, resolution 1.89Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7ur2 is a 8 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.89Å Ligands: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function KALRN_MOUSE Promotes the exchange of GDP by GTP. Activates specific Rho GTPase family members, thereby inducing various signaling mechanisms that regulate neuronal shape, growth, and plasticity, through their effects on the actin cytoskeleton. Induces lamellipodia independent of its GEF activity (By similarity).[UniProtKB:P97924] Publication Abstract from PubMed Gated entry of lipophilic ligands into the enclosed hydrophobic pocket in stand-alone Sec14 domain proteins often links lipid metabolism to membrane trafficking. Similar domains occur in multidomain mammalian proteins that activate small GTPases and regulate actin dynamics. The neuronal RhoGEF Kalirin, a central regulator of cytoskeletal dynamics, contains a Sec14 domain (Kal(bSec14)) followed by multiple spectrin-like repeats and catalytic domains. Previous studies demonstrated that Kalirin lacking its Sec14 domain fails to maintain cell morphology or dendritic spine length, yet whether and how Kal(bSec14) interacts with lipids remain unknown. Here, we report the structural and biochemical characterization of Kal(bSec14). Kal(bSec14) adopts a closed conformation, sealing off the canonical ligand entry site, and instead employs a surface groove to bind a limited set of lysophospholipids. The low-affinity interactions of Kal(bSec14) with lysolipids are expected to serve as a general model for the regulation of Rho signaling by other Sec14-containing Rho activators. Structure of the Sec14 domain of Kalirin reveals a distinct class of lipid-binding module in RhoGEFs.,Li Y, Pustovalova Y, Doukov TI, Hoch JC, Mains RE, Eipper BA, Hao B Nat Commun. 2023 Jan 6;14(1):96. doi: 10.1038/s41467-022-35678-4. PMID:36609407 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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