2BN2

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

Replaces:  1BN2

Summary for 2BN2

• Entry DOI: 10.2210/pdb2bn2/pdb
• Related: 1NPO
• Descriptor: NEUROPHYSIN II, PHENYLALANINE, TYROSINE (3 entities in total)
• Functional Keywords: hormone packaging, transport, protein-peptide complex, hormone
• Biological source: Bos taurus (cattle)
• Cellular location: Secreted: P01180
• Total number of polymer chains: 4
• Total formula weight: 40946.52

Authors

Rose, J.P.,Wang, B.C. (deposition date: 1998-12-18, release date: 1999-02-16, Last modification date: 2024-10-30)

Primary citation

Chen, L.Q.,Rose, J.P.,Breslow, E.,Yang, D.,Chang, W.R.,Furey Jr., W.F.,Sax, M.,Wang, B.C.
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.
Proc.Natl.Acad.Sci.USA, 88:4240-4244, 1991

PubMed Abstract: 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.

PubMed: 2034668
DOI: 10.1073/pnas.88.10.4240

Experimental method

X-RAY DIFFRACTION (2.8 Å)