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PDBsum entry 2bf9
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protein metals links
Hormone PDB id
2bf9

 

 

 

 

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Contents
Protein chain
36 a.a. *
Metals
_ZN
Waters ×82
* Residue conservation analysis
PDB id:
2bf9
Name: Hormone
Title: Anisotropic refinement of avian (turkey) pancreatic polypeptide at 0. 99 angstroms resolution.
Structure: Pancreatic hormone. Chain: a. Synonym: avian pancreatic polypeptide, pp, pancreatic polypeptide. Other_details: complex with zn(ii) ion.
Source: Meleagris gallopavo. Domestic turkey. Organism_taxid: 9103. Organ: pancreas. Cell: islets of langerhans. Other_details: collected from commercial uk turkey farm.
Biol. unit: Dimer (from PDB file)
Resolution:
0.99Å     R-factor:   0.137     R-free:   0.179
Authors: I.Tickle,I.Glover,J.Pitts,S.Wood,T.L.Blundell
Key ref: I.Glover et al. (1983). Conformational flexibility in a small globular hormone: x-ray analysis of avian pancreatic polypeptide at 0.98-A resolution. Biopolymers, 22, 293-304. PubMed id: 6673760
Date:
06-Dec-04     Release date:   08-Dec-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P68249  (PAHO_MELGA) -  Pancreatic polypeptide from Meleagris gallopavo
Seq:
Struc: 		36 a.a.
36 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
Biopolymers 22:293-304 (1983)
PubMed id: 6673760  
 
 
Conformational flexibility in a small globular hormone: x-ray analysis of avian pancreatic polypeptide at 0.98-A resolution.
I.Glover, I.Haneef, J.Pitts, S.Wood, D.Moss, I.Tickle, T.Blundell.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

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The solution structure of pGolemi, a high affinity Mena EVH1 binding miniature protein, suggests explanations for paralog-specific binding to Ena/VASP homology (EVH) 1 domains.
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PDB code: 2k76
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Grafting miniature DNA binding proteins.
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11668539 J.W.Chin, and A.Schepartz (2001).
Design and Evolution of a Miniature Bcl-2 Binding Protein We thank the HHMI Biopolymer/Keck Foundation Biotechnology Resource Laboratory (Yale University School of Medicine, New Haven, CT) for oligonucleotide and peptide synthesis and amino acid analysis and Professor Jennifer Doudna (Yale University) for use of a Perseptive Voyager-DE (MALDI-TOF) mass spectrometer. We are grateful also to Dr. Junying Yuan and Dr. Alexi Degterev (Harvard Medical School) for a generous gift of Bcl-X(L)-His(6) and Stacey E. Rutledge for helpful comments. This work was supported by the National Institutes of Health.
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10089313 M.Mukherjee (1999).
Ab initio structure determination of a small protein, rubredoxin, by direct methods.
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9600887 C.Keasar, D.Tobi, R.Elber, and J.Skolnick (1998).
Coupling the folding of homologous proteins.
  Proc Natl Acad Sci U S A, 95, 5880-5883.  
9824454 C.P.Tensen, K.J.Cox, J.F.Burke, R.Leurs, R.C.van der Schors, W.P.Geraerts, E.Vreugdenhil, and H.Heerikhuizen (1998).
Molecular cloning and characterization of an invertebrate homologue of a neuropeptide Y receptor.
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10089502 M.Vlassi, Z.Dauter, K.S.Wilson, and M.Kokkinidis (1998).
Structural parameters for proteins derived from the atomic resolution (1.09 A) structure of a designed variant of the ColE1 ROP protein.
  Acta Crystallogr D Biol Crystallogr, 54, 1245-1260.
PDB code: 1nkd
  9672837 N.Benhabilès, X.Gallet, A.Thomas-Soumarmon, and R.Brasseur (1998).
A descriptive analysis of populations of three-dimensional structures calculated from primary sequences of proteins by OSIRIS.
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9029504 N.Ingenhoven, and A.G.Beck-Sickinger (1997).
Fluorescent labelled analogues of neuropeptide Y for the characterization of cells expressing NPY receptor subtypes.
  J Recept Signal Transduct Res, 17, 407-418.  
9231326 M.Gurrath, A.Bisello, K.Bottazzo, C.W.Chung, S.Mammi, and E.Peggion (1996).
Conformational analysis of neuropeptide Y segments by CD, NMR spectroscopy and restrained molecular dynamics.
  J Pept Sci, 2, 176-193.  
  8743297 Y.J.Deng, G.C.Andrews, and F.Karush (1996).
Epitopic characterization of neuropeptide Y (NPY) by alanine-scanning mutagenesis.
  Hybridoma, 15, 159-162.  
7893945 A.G.Beck-Sickinger, and G.Jung (1995).
Structure-activity relationships of neuropeptide Y analogues with respect to Y1 and Y2 receptors.
  Biopolymers, 37, 123-142.  
8903958 A.G.Beck-Sickinger, H.A.Wieland, and J.Brunner (1995).
Synthesis, receptor binding, and crosslinking of photoactive analogues of neuropeptide Y.
  J Recept Signal Transduct Res, 15, 473-485.  
8592703 H.Zhang, C.F.Wong, T.Thacher, and H.Rabitz (1995).
Parametric sensitivity analysis of avian pancreatic polypeptide (APP).
  Proteins, 23, 218-232.  
7766824 S.S.Chu, D.V.Velde, D.Shobe, P.Balse, and M.B.Doughty (1995).
Conformational properties of the proline region of porcine neuropeptide Y by CD and 1H-nmr spectroscopy.
  Biopolymers, 35, 583-593.  
8527647 S.Sun (1995).
A genetic algorithm that seeks native states of peptides and proteins.
  Biophys J, 69, 340-355.  
8749366 Z.Dauter, V.S.Lamzin, and K.S.Wilson (1995).
Proteins at atomic resolution.
  Curr Opin Struct Biol, 5, 784-790.  
7957231 A.G.Beck-Sickinger, H.A.Wieland, H.Wittneben, K.D.Willim, K.Rudolf, and G.Jung (1994).
Complete L-alanine scan of neuropeptide Y reveals ligands binding to Y1 and Y2 receptors with distinguished conformations.
  Eur J Biochem, 225, 947-958.  
7773780 C.Toniolo, C.Peggion, M.Crisma, F.Formaggio, X.Shui, and D.S.Eggleston (1994).
Structure determination of racemic trichogin A IV using centrosymmetric crystals.
  Nat Struct Biol, 1, 908-914.  
  8251944 A.Liwo, M.R.Pincus, R.J.Wawak, S.Rackovsky, and H.A.Scheraga (1993).
Prediction of protein conformation on the basis of a search for compact structures: test on avian pancreatic polypeptide.
  Protein Sci, 2, 1715-1731.  
8364154 M.B.Doughty, and L.Hu (1993).
The contribution of helical potential to the in vitro receptor binding activity of a neuropeptide Y N-terminal deletion fragment.
  Biopolymers, 33, 1195-1206.  
8461457 M.Hollósi, L.Otvös, L.Urge, J.Kajtár, A.Perczel, I.Laczkó, Z.Vadász, and G.D.Fasman (1993).
Ca(2+)-induced conformational transitions of phosphorylated peptides.
  Biopolymers, 33, 497-510.  
  8495198 S.Sun (1993).
Reduced representation model of protein structure prediction: statistical potential and genetic algorithms.
  Protein Sci, 2, 762-785.  
8427934 S.Vajda, M.S.Jafri, O.U.Sezerman, and C.DeLisi (1993).
Necessary conditions for avoiding incorrect polypeptide folds in conformational search by energy minimization.
  Biopolymers, 33, 173-192.  
1316841 D.F.Mierke, H.Dürr, H.Kessler, and G.Jung (1992).
Neuropeptide Y. Optimized solid-phase synthesis and conformational analysis in trifluoroethanol.
  Eur J Biochem, 206, 39-48.  
1425680 H.Darbon, J.M.Bernassau, C.Deleuze, J.Chenu, A.Roussel, and C.Cambillau (1992).
Solution conformation of human neuropeptide Y by 1H nuclear magnetic resonance and restrained molecular dynamics.
  Eur J Biochem, 209, 765-771.  
1524828 S.M.Rajpara, P.D.Garcia, R.Roberts, J.C.Eliassen, D.F.Owens, D.Maltby, R.M.Myers, and E.Mayeri (1992).
Identification and molecular cloning of a neuropeptide Y homolog that produces prolonged inhibition in Aplysia neurons.
  Neuron, 9, 505-513.  
  1690703 A.B.Hartman, M.Venkatesan, E.V.Oaks, and J.M.Buysse (1990).
Sequence and molecular characterization of a multicopy invasion plasmid antigen gene, ipaH, of Shigella flexneri.
  J Bacteriol, 172, 1905-1915.  
2361157 G.M.Crippen, and M.E.Snow (1990).
A 1.8 A resolution potential function for protein folding.
  Biopolymers, 29, 1479-1489.  
2328293 H.Minakata, and T.Iwashita (1990).
Synthesis of analogues of peptide YY with modified N-terminal regions: relationships of amphiphilic secondary structures and activity in rat vas deferens.
  Biopolymers, 29, 61-67.  
2248480 J.H.Boublik, M.A.Spicer, N.A.Scott, M.R.Brown, and J.E.Rivier (1990).
Biologically active neuropeptide Y analogs.
  Ann N Y Acad Sci, 611, 27-34.  
2248486 J.M.Allen (1990).
Molecular structure of neuropeptide Y.
  Ann N Y Acad Sci, 611, 86-98.  
2174224 R.Quirion, J.C.Martel, Y.Dumont, A.Cadieux, F.Jolicoeur, S.St-Pierre, and A.Fournier (1990).
Neuropeptide Y receptors: autoradiographic distribution in the brain and structure-activity relationships.
  Ann N Y Acad Sci, 611, 58-72.  
2174222 T.W.Schwartz, J.Fuhlendorff, L.L.Kjems, M.S.Kristensen, M.Vervelde, M.O'Hare, J.L.Krstenansky, and B.Bjørnholm (1990).
Signal epitopes in the three-dimensional structure of neuropeptide Y. Interaction with Y1, Y2, and pancreatic polypeptide receptors.
  Ann N Y Acad Sci, 611, 35-47.  
2543973 J.L.Krstenansky, T.J.Owen, S.H.Buck, K.A.Hagaman, and L.R.McLean (1989).
Centrally truncated and stabilized porcine neuropeptide Y analogs: design, synthesis, and mouse brain receptor binding.
  Proc Natl Acad Sci U S A, 86, 4377-4381.  
3199149 A.D.MacKerell (1988).
Molecular modeling and dynamics of neuropeptide Y.
  J Comput Aided Mol Des, 2, 55-63.  
3031687 J.Allen, J.Novotný, J.Martin, and G.Heinrich (1987).
Molecular structure of mammalian neuropeptide Y: analysis by molecular cloning and computer-aided comparison with crystal structure of avian homologue.
  Proc Natl Acad Sci U S A, 84, 2532-2536.  
3471111 H.J.Berendsen, W.F.Van Gunsteren, H.R.Zwinderman, and R.G.Geurtsen (1986).
Simulations of proteins in water.
  Ann N Y Acad Sci, 482, 269-286.  
2992954 G.M.Clore, A.M.Gronenborn, and L.W.McLaughlin (1985).
The structure of the double-stranded RNA pentamer 5'(CACAG) . 5'(CUGUG) determined by nuclear Overhauser enhancement measurements: interproton distance determination and structure refinement on the basis of X-ray coordinates.
  Eur J Biochem, 151, 153-165.  
3986295 T.Noguti, and N.Go (1985).
Efficient Monte Carlo method for simulation of fluctuating conformations of native proteins.
  Biopolymers, 24, 527-546.  
6745282 I.D.Glover, D.J.Barlow, J.E.Pitts, S.P.Wood, I.J.Tickle, T.L.Blundell, K.Tatemoto, J.R.Kimmel, A.Wollmer, and W.Strassburger (1984).
Conformational studies on the pancreatic polypeptide hormone family.
  Eur J Biochem, 142, 379-385.  
6646210 T.Blundell, D.Barlow, N.Borkakoti, and J.Thornton (1983).
Solvent-induced distortions and the curvature of alpha-helices.
  Nature, 306, 281-283.  
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 code is shown on the right.

 

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