2bn2 | pdb_00002bn2

CRYSTAL STRUCTURE OF BOVINE NEUROPHYSIN II COMPLEXED WITH THE VASOPRESSIN ANALOGUE PHE-TYR AMIDE

spinqualitylabelsall models 2bn2, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2bn2 is a 4 chain structure with sequence from Bos taurus. This structure supersedes the now removed PDB entry 1bn2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: PHE, TYR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NEU2_BOVIN Neurophysin 2 specifically binds vasopressin. Vasopressin has a direct antidiuretic action on the kidney, it also causes vasoconstriction of the peripheral vessels. 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 The crystal structure of a dipeptide complex of bovine neurophysin II has been solved at 2.8 A resolution solely by using single-wavelength anomalous scattering data from a single iodinated derivative. The asymmetric unit is an elongated tetramer of dimensions 110 x 40 x 30 A, composed of two dimers related by pseudo twofold symmetry. Each monomer consists of two homologous layers, each with four antiparallel beta-strands. The two regions are connected by a helix followed by a long loop. Monomer-monomer contacts involve antiparallel beta-sheet interactions, which form a dimer with two layers of eight beta-strands. One peptide per monomer occupies the principal hormone-binding pocket formed by part of the amino-terminal region and parts of the connecting helix and loop, with binding to protein consistent with conclusions drawn from solution studies. Dimer-dimer contacts involve the Tyr49 region adjacent to this site. A fifth dipeptide, of unknown biological significance, helps to stabilize one of the monomer-monomer interfaces and the tetramer-tetramer network in the crystal. Crystal structure of a bovine neurophysin II dipeptide complex at 2.8 A determined from the single-wavelength anomalous scattering signal of an incorporated iodine atom.,Chen LQ, Rose JP, Breslow E, Yang D, Chang WR, Furey WF Jr, Sax M, Wang BC Proc Natl Acad Sci U S A. 1991 May 15;88(10):4240-4. PMID:2034668 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Neurophysin

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