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PDBsum entry 2bn2
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protein ligands Protein-protein interface(s) links
Hormone PDB id
2bn2

 

 

 

 

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Contents
Protein chains
85 a.a. *
79 a.a. *
Ligands
PHE-TYR ×4
* Residue conservation analysis
PDB id:
2bn2
Name: Hormone
Title: Crystal structure of bovine neurophysin ii complexed with the vasopressin analogue phe-tyr amide
Structure: Neurophysin ii. Chain: a, c, e, g. Synonym: bnpii
Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: posterior pituitary
Biol. unit: Dimer (from PDB file)
Resolution:
2.80Å     R-factor:   0.208     R-free:   0.262
Authors: J.P.Rose,B.C.Wang
Key ref: L.Q.Chen et al. (1991). 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 U S A, 88, 4240-4244. PubMed id: 2034668 DOI: 10.1073/pnas.88.10.4240
Date:
18-Dec-98     Release date:   16-Feb-99    
Supersedes: 1bn2
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01180  (NEU2_BOVIN) -  Vasopressin-neurophysin 2-copeptin from Bos taurus
Seq:
Struc: 		166 a.a.
85 a.a.
Protein chains
Pfam   ArchSchema ?
P01180  (NEU2_BOVIN) -  Vasopressin-neurophysin 2-copeptin from Bos taurus
Seq:
Struc: 		166 a.a.
79 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1073/pnas.88.10.4240 Proc Natl Acad Sci U S A 88:4240-4244 (1991)
PubMed id: 2034668  
 
 
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.
L.Q.Chen, J.P.Rose, E.Breslow, D.Yang, W.R.Chang, W.F.Furey, M.Sax, B.C.Wang.
 
  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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19830265 D.R.Cool, S.B.Jackson, and K.S.Waddell (2008).
Structural Requirements for Sorting Pro-Vasopressin to the Regulated Secretory Pathway in a Neuronal Cell Line.
  Open Neuroendocrinol J, 1, 1-8.  
18316733 E.Stafflinger, K.K.Hansen, F.Hauser, M.Schneider, G.Cazzamali, M.Williamson, and C.J.Grimmelikhuijzen (2008).
Cloning and identification of an oxytocin/vasopressin-like receptor and its ligand from insects.
  Proc Natl Acad Sci U S A, 105, 3262-3267.  
17192588 X.Li, H.Lee, J.Wu, and E.Breslow (2007).
Contributions of the interdomain loop, amino terminus, and subunit interface to the ligand-facilitated dimerization of neurophysin: crystal structures and mutation studies of bovine neurophysin-I.
  Protein Sci, 16, 52-68.
PDB codes: 2hnu 2hnv 2hnw
16075380 B.J.Zhang, M.Yamashita, R.Fields, K.Kusano, and H.Gainer (2005).
EGFP-tagged vasopressin precursor protein sorting into large dense core vesicles and secretion from PC12 cells.
  Cell Mol Neurobiol, 25, 581-605.  
15983419 H.Xu, C.Yang, L.Chen, I.A.Kataeva, W.Tempel, D.Lee, J.E.Habel, D.Nguyen, J.W.Pflugrath, J.D.Ferrara, W.B.Arendall, J.S.Richardson, D.C.Richardson, Z.J.Liu, M.G.Newton, J.P.Rose, and B.C.Wang (2005).
Away from the edge II: in-house Se-SAS phasing with chromium radiation.
  Acta Crystallogr D Biol Crystallogr, 61, 960-966.
PDB code: 1xho
16131750 J.Ondrácek, M.S.Weiss, J.Brynda, J.Fiala, F.Jursík, P.Rezácová, L.B.Jenner, and J.Sedlácek (2005).
Regular arrangement of periodates bound to lysozyme.
  Acta Crystallogr D Biol Crystallogr, 61, 1181-1189.
PDB code: 1hc0
15735337 T.C.Appleby, G.Larson, I.W.Cheney, H.Walker, J.Z.Wu, W.Zhong, Z.Hong, and N.Yao (2005).
Structure of human uridine-cytidine kinase 2 determined by SIRAS using a rotating-anode X-ray generator and a single samarium derivative.
  Acta Crystallogr D Biol Crystallogr, 61, 278-284.
PDB code: 1xrj
14678298 J.H.Christensen, C.Siggaard, T.J.Corydon, G.L.Robertson, N.Gregersen, L.Bolund, and S.Rittig (2004).
Impaired trafficking of mutated AVP prohormone in cells expressing rare disease genes causing autosomal dominant familial neurohypophyseal diabetes insipidus.
  Clin Endocrinol (Oxf), 60, 125-136.  
14573949 C.Yang, J.W.Pflugrath, D.A.Courville, C.N.Stence, and J.D.Ferrara (2003).
Away from the edge: SAD phasing from the sulfur anomalous signal measured in-house with chromium radiation.
  Acta Crystallogr D Biol Crystallogr, 59, 1943-1957.  
12499540 I.Usón, B.Schmidt, R.von Bülow, S.Grimme, K.von Figura, M.Dauter, K.R.Rajashankar, Z.Dauter, and G.M.Sheldrick (2003).
Locating the anomalous scatterer substructures in halide and sulfur phasing.
  Acta Crystallogr D Biol Crystallogr, 59, 57-66.
PDB codes: 1e6f 1gqb
14510916 P.C.Elias, L.L.Elias, N.Torres, A.C.Moreira, J.Antunes-Rodrigues, and M.Castro (2003).
Progressive decline of vasopressin secretion in familial autosomal dominant neurohypophyseal diabetes insipidus presenting a novel mutation in the vasopressin-neurophysin II gene.
  Clin Endocrinol (Oxf), 59, 511-518.  
11752774 E.Girard, L.Chantalat, J.Vicat, and R.Kahn (2002).
Gd-HPDO3A, a complex to obtain high-phasing-power heavy-atom derivatives for SAD and MAD experiments: results with tetragonal hen egg-white lysozyme.
  Acta Crystallogr D Biol Crystallogr, 58, 1-9.
PDB code: 1h87
12037324 E.K.Leinala, P.L.Davies, and Z.Jia (2002).
Elevated temperature and tyrosine iodination aid in the crystallization and structure determination of an antifreeze protein.
  Acta Crystallogr D Biol Crystallogr, 58, 1081-1083.  
12037300 G.Evans, and G.Bricogne (2002).
Triiodide derivatization and combinatorial counter-ion replacement: two methods for enhancing phasing signal using laboratory Cu Kalpha X-ray equipment.
  Acta Crystallogr D Biol Crystallogr, 58, 976-991.
PDB codes: 1gw9 1gwa 1gwd 1gwg
12077434 J.A.Gavira, D.Toh, J.Lopéz-Jaramillo, J.M.García-Ruíz, and J.D.Ng (2002).
Ab initio crystallographic structure determination of insulin from protein to electron density without crystal handling.
  Acta Crystallogr D Biol Crystallogr, 58, 1147-1154.  
11980496 T.L.Nguyen, and E.Breslow (2002).
NMR analysis of the monomeric form of a mutant unliganded bovine neurophysin: comparison with the crystal structure of a neurophysin dimer.
  Biochemistry, 41, 5920-5930.
PDB codes: 1l5c 1l5d
11856836 Z.Dauter, M.Dauter, and E.Dodson (2002).
Jolly SAD.
  Acta Crystallogr D Biol Crystallogr, 58, 494-506.  
11514677 C.K.Wu, B.Hu, J.P.Rose, Z.J.Liu, T.L.Nguyen, C.Zheng, E.Breslow, and B.C.Wang (2001).
Structures of an unliganded neurophysin and its vasopressin complex: implications for binding and allosteric mechanisms.
  Protein Sci, 10, 1869-1880.
PDB codes: 1jk4 1jk6
11222771 V.Tereshko, C.J.Wilds, G.Minasov, T.P.Prakash, M.A.Maier, A.Howard, Z.Wawrzak, M.Manoharan, and M.Egli (2001).
Detection of alkali metal ions in DNA crystals using state-of-the-art X-ray diffraction experiments.
  Nucleic Acids Res, 29, 1208-1215.
PDB codes: 1i0f 1i0g 1i0j 1i0k 1i0m 1i0n 1i0o 1i0p 1i0q 1i0t
11418767 Z.Dauter, and D.A.Adamiak (2001).
Anomalous signal of phosphorus used for phasing DNA oligomer: importance of data redundancy.
  Acta Crystallogr D Biol Crystallogr, 57, 990-995.
PDB code: 1ick
11250204 Z.Dauter, and M.Dauter (2001).
Entering a new phase: using solvent halide ions in protein structure determination.
  Structure, 9, R21-R26.  
10739916 D.E.Brodersen, E.de La Fortelle, C.Vonrhein, G.Bricogne, J.Nyborg, and M.Kjeldgaard (2000).
Applications of single-wavelength anomalous dispersion at high and atomic resolution.
  Acta Crystallogr D Biol Crystallogr, 56, 431-441.  
10844588 F.M.de Bree (2000).
Trafficking of the vasopressin and oxytocin prohormone through the regulated secretory pathway.
  J Neuroendocrinol, 12, 589-594.  
10891091 S.Eubanks, T.L.Nguyen, D.Peyton, and E.Breslow (2000).
Modulation of dimerization, binding, stability, and folding by mutation of the neurophysin subunit interface.
  Biochemistry, 39, 8085-8094.  
11038011 Y.Iwasaki, Y.Oiso, H.Saito, and J.A.Majzoub (2000).
Effects of various mutations in the neurophysin/glycopeptide portion of the vasopressin gene on vasopressin expression in vitro.
  Tohoku J Exp Med, 191, 187-202.  
10666615 Z.Dauter, M.Dauter, and K.R.Rajashankar (2000).
Novel approach to phasing proteins: derivatization by short cryo-soaking with halides.
  Acta Crystallogr D Biol Crystallogr, 56, 232-237.  
  10211828 E.Breslow, V.Mombouyran, R.Deeb, C.Zheng, J.P.Rose, B.C.Wang, and R.H.Haschemeyer (1999).
Structural basis of neurophysin hormone specificity: Geometry, polarity, and polarizability in aromatic ring interactions.
  Protein Sci, 8, 820-831.  
  10422844 M.Archer, A.L.Carvalho, S.Teixeira, I.Moura, J.J.Moura, F.Rusnak, and M.J.Romão (1999).
Structural studies by X-ray diffraction on metal substituted desulforedoxin, a rubredoxin-type protein.
  Protein Sci, 8, 1536-1545.
PDB codes: 1cfw 1dcd 1dhg
9109434 M.Ito, J.L.Jameson, and M.Ito (1997).
Molecular basis of autosomal dominant neurohypophyseal diabetes insipidus. Cellular toxicity caused by the accumulation of mutant vasopressin precursors within the endoplasmic reticulum.
  J Clin Invest, 99, 1897-1905.  
8794757 C.Zheng, S.Cahill, and E.Breslow (1996).
The behavior of the active site salt bridge of bovine neurophysins as monitored by 15N NMR spectroscopy and chemical substitution. Relationship to biochemical properties.
  Biochemistry, 35, 11763-11772.  
8945633 G.Olias, D.Richter, and H.Schmale (1996).
Heterologous expression of human vasopressin-neurophysin precursors in a pituitary cell line: defective transport of a mutant protein from patients with familial diabetes insipidus.
  DNA Cell Biol, 15, 929-935.  
8547267 R.Deeb, and E.Breslow (1996).
Thermodynamic role of the pro region of the neurophysin precursor in neurophysin folding: evidence from the effects of ligand peptides on folding.
  Biochemistry, 35, 864-873.  
  8554046 S.Rittig, G.L.Robertson, C.Siggaard, L.Kovács, N.Gregersen, J.Nyborg, and E.B.Pedersen (1996).
Identification of 13 new mutations in the vasopressin-neurophysin II gene in 17 kindreds with familial autosomal dominant neurohypophyseal diabetes insipidus.
  Am J Hum Genet, 58, 107-117.  
7541187 T.M.Fujiwara, K.Morgan, and D.G.Bichet (1995).
Molecular biology of diabetes insipidus.
  Annu Rev Med, 46, 331-343.  
1544459 A.V.Efimov (1992).
A novel super-secondary structure of beta-proteins. A triple-strand corner.
  FEBS Lett, 298, 261-265.  
1379721 J.Heierhorst, K.Lederis, and D.Richter (1992).
Presence of a member of the Tc1-like transposon family from nematodes and Drosophila within the vasotocin gene of a primitive vertebrate, the Pacific hagfish Eptatretus stouti.
  Proc Natl Acad Sci U S A, 89, 6798-6802.  
1584795 R.E.van Kesteren, A.B.Smit, R.W.Dirks, N.D.de With, W.P.Geraerts, and J.Joosse (1992).
Evolution of the vasopressin/oxytocin superfamily: characterization of a cDNA encoding a vasopressin-related precursor, preproconopressin, from the mollusc Lymnaea stagnalis.
  Proc Natl Acad Sci U S A, 89, 4593-4597.  
  1740104 U.Bahnsen, P.Oosting, D.F.Swaab, P.Nahke, D.Richter, and H.Schmale (1992).
A missense mutation in the vasopressin-neurophysin precursor gene cosegregates with human autosomal dominant neurohypophyseal diabetes insipidus.
  EMBO J, 11, 19-23.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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