2bn2
From Proteopedia
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CRYSTAL STRUCTURE OF BOVINE NEUROPHYSIN II COMPLEXED WITH THE VASOPRESSIN ANALOGUE PHE-TYR AMIDE
Overview
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.
About this Structure
2BN2 is a Single protein structure of sequence from Bos taurus. This structure superseeds the now removed PDB entry 1BN2. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Nov 21 08:50:16 2007
