7jny | pdb_00007jny

Crystal structure of CXCL13

spinqualitylabelsall models 7jny, resolution 1.88Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7jny is a 1 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 4zai. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.88Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CXL13_HUMAN Chemotactic for B-lymphocytes but not for T-lymphocytes, monocytes and neutrophils. Does not induce calcium release in B-lymphocytes. Binds to BLR1/CXCR5. Publication Abstract from PubMed CXCL13 is the cognate chemokine agonist of CXCR5, a class A G-protein-coupled receptor (GPCR) that is essential for proper humoral immune responses. Using a `methionine scanning' mutagenesis method on the N-terminus of CXCL13, which is the chemokine signaling region, it was shown that minor length alterations and side-chain substitutions still result in CXCR5 activation. This observation indicates that the orthosteric pocket of CXCR5 can tolerate these changes without severely affecting the activity. The introduction of bulk on the ligand was well tolerated by the receptor, whereas a loss of contacts was less tolerated. Furthermore, two crystal structures of CXCL13 mutants were solved, both of which represent the first uncomplexed structures of the human protein. These structures were stabilized by unique interactions formed by the N-termini of the ligands, indicating that CXCL13 exhibits substantial N-terminal flexibility while the chemokine core domain remains largely unchanged. Additionally, it was observed that CXCL13 harbors a large degree of flexibility in the C-terminal extension of the ligand. Comparisons with other published structures of human and murine CXCL13 validate the relative rigidity of the core domain as well as the N- and C-terminal mobilities. Collectively, these mutants and their structures provide the field with additional insights into how CXCL13 interacts with CXCR5. The N-terminal length and side-chain composition of CXCL13 affect crystallization, structure and functional activity.,Rosenberg EM Jr, Herrington J, Rajasekaran D, Murphy JW, Pantouris G, Lolis EJ Acta Crystallogr D Struct Biol. 2020 Oct 1;76(Pt 10):1033-1049. doi:, 10.1107/S2059798320011687. Epub 2020 Sep 25. PMID:33021505 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also C-X-C motif chemokine 3D structures

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