6ith | pdb_00006ith

Structure of the transmembrane domain of syndecan 2 in micelles

spinqualitylabelsall models 6ith, 15 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ith is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SDC2_HUMAN] Cell surface proteoglycan that bears heparan sulfate. Regulates dendritic arbor morphogenesis (By similarity). Publication Abstract from PubMed Syndecans are single-span membrane proteins playing important roles in cell-cell and cell-matrix interactions. The transmembrane domain of syndecans is critical for signal transduction across the cell membrane. Here, the structure of the transmembrane domain of syndecan-2 in detergent micelles was investigated using solution NMR spectroscopy. Backbone resonance assignment was obtained, and NMR studies show that the transmembrane domain forms a helix in detergent micelles, which is also supported by the hydrogen and deuterium exchange experiment. A study of the dynamics revealed the rigid structure of the transmembrane domain formed in solution, and paramagnetic relaxation enhancement defined the topology of the transmembrane domain in detergent micelles. This structural analysis may facilitate a better understanding of the role of the syndecan-2 transmembrane domain in signal transduction. Secondary structure and topology of the transmembrane domain of Syndecan-2 in detergent micelles.,Li Q, Ng HQ, Kang C FEBS Lett. 2019 Feb 11. doi: 10.1002/1873-3468.13335. PMID:30742705 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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