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| {{STRUCTURE_2bn2| PDB=2bn2 | SCENE= }} | | {{STRUCTURE_2bn2| PDB=2bn2 | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF BOVINE NEUROPHYSIN II COMPLEXED WITH THE VASOPRESSIN ANALOGUE PHE-TYR AMIDE'''
| | ===CRYSTAL STRUCTURE OF BOVINE NEUROPHYSIN II COMPLEXED WITH THE VASOPRESSIN ANALOGUE PHE-TYR AMIDE=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_2034668}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 2034668 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_2034668}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Hormone packaging]] | | [[Category: Hormone packaging]] |
| [[Category: Transport]] | | [[Category: Transport]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:56:56 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:21:10 2008'' |
