1cfb

CRYSTAL STRUCTURE OF TANDEM TYPE III FIBRONECTIN DOMAINS FROM DROSOPHILA NEUROGLIAN AT 2.0 ANGSTROMS

spinqualitylabelsall models 1cfb, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1cfb is a 1 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NA, NAG, SO4 Gene: POTENTIAL (DROME) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [NRG_DROME] The long isoform may play a role in neural and glial cell adhesion in the developing embryo. The short isoform may be a more general cell adhesion molecule involved in other tissues and imaginal disk morphogenesis. Vital for embryonic development. Essential for septate junctions. Septate junctions, which are the equivalent of vertebrates tight junctions, are characterized by regular arrays of transverse structures that span the intermembrane space and form a physical barrier to diffusion. Required for the blood-brain barrier formation. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed We report the crystal structure of two adjacent fibronectin type III repeats from the Drosophila neural cell adhesion molecule neuroglian. Each domain consists of two antiparallel beta sheets and is folded topologically identically to single fibronectin type III domains from the extracellular matrix proteins tenascin and fibronectin. beta bulges and left-handed polyproline II helices disrupt the regular beta sheet structure of both neuroglian domains. The hydrophobic interdomain interface includes a metal-binding site, presumably involved in stabilizing the relative orientation between domains and predicted by sequence comparision to be present in the vertebrate homolog molecule L1. The neuroglian domains are related by a near perfect 2-fold screw axis along the longest molecular dimension. Using this relationship, a model for arrays of tandem fibronectin type III repeats in neuroglian and other molecules is proposed. Crystal structure of tandem type III fibronectin domains from Drosophila neuroglian at 2.0 A.,Huber AH, Wang YM, Bieber AJ, Bjorkman PJ Neuron. 1994 Apr;12(4):717-31. PMID:7512815 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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