6tpu

Crystal structures of FNIII domain three and four of the human leucocyte common antigen-related protein, LAR

spinqualitylabelsall models 6tpu, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6tpu is a 2 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 1.55Å Ligands: CL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PTPRF_HUMAN Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase). The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Publication Abstract from PubMed Leucocyte common antigen-related protein (LAR) is a post-synaptic type I transmembrane receptor protein that is important for neuronal functionality and is genetically coupled to neuronal disorders such as attention deficit hyperactivity disorder (ADHD). To understand the molecular function of LAR, structural and biochemical studies of protein fragments derived from the ectodomain of human LAR have been performed. The crystal structure of a fragment encompassing the first four FNIII domains (LAR(FN1-4)) showed a characteristic L shape. SAXS data suggested limited flexibility within LAR(FN1-4), while rigid-body refinement of the SAXS data using the X-ray-derived atomic model showed a smaller angle between the domains defining the L shape compared with the crystal structure. The capabilities of the individual LAR fragments to interact with heparin was examined using microscale thermophoresis and heparin-affinity chromatography. The results showed that the three N-terminal immunoglobulin domains (LAR(Ig1-3)) and the four C-terminal FNIII domains (LAR(FN5-8)) both bound heparin, while LAR(FN1-4) did not. The low-molecular-weight heparin drug Innohep induced a shift in hydrodynamic volume as assessed by size-exclusion chromatography of LAR(Ig1-3) and LAR(FN5-8), while the chemically defined pentameric heparin drug Arixtra did not. Together, the presented results suggest the presence of an additional heparin-binding site in human LAR. Crystal and solution structures of fragments of the human leucocyte common antigen-related protein.,Vilstrup J, Simonsen A, Birkefeldt T, Strandbygard D, Lyngso J, Pedersen JS, Thirup S Acta Crystallogr D Struct Biol. 2020 May 1;76(Pt 5):406-417. doi:, 10.1107/S2059798320003885. Epub 2020 Apr 15. PMID:32355037 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tyrosine phosphatase 3D structures

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