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PDBsum entry 1zwc

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protein links
Hormone PDB id
1zwc
Jmol
Contents
Protein chain
37 a.a. *
* Residue conservation analysis
PDB id:
1zwc
Name: Hormone
Title: Structure of bovine parathyroid hormone fragment 1-37, nmr, 10 structures
Structure: Parathyroid hormone. Chain: a. Fragment: 1 - 37. Synonym: bpth(1-37). Engineered: yes
Source: Bos taurus. Cattle. Organism_taxid: 9913. Gene: potential
NMR struc: 10 models
Authors: P.Roesch,U.C.Marx
Key ref: U.C.Marx et al. (2000). Solution structures of human parathyroid hormone fragments hPTH(1-34) and hPTH(1-39) and bovine parathyroid hormone fragment bPTH(1-37). Biochem Biophys Res Commun, 267, 213-220. PubMed id: 10623601 DOI: 10.1006/bbrc.1999.1958
Date:
17-Jun-96     Release date:   12-Mar-97    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01268  (PTHY_BOVIN) -  Parathyroid hormone
Seq:
Struc:
115 a.a.
37 a.a.
Key:    PfamA domain  Secondary structure

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biochemical function     hormone activity     1 term  

 

 
DOI no: 10.1006/bbrc.1999.1958 Biochem Biophys Res Commun 267:213-220 (2000)
PubMed id: 10623601  
 
 
Solution structures of human parathyroid hormone fragments hPTH(1-34) and hPTH(1-39) and bovine parathyroid hormone fragment bPTH(1-37).
U.C.Marx, K.Adermann, P.Bayer, W.G.Forssmann, P.Rösch.
 
  ABSTRACT  
 
Parathyroid hormone (PTH) is involved in regulation of the calcium level in blood and has an influence on bone metabolism, thus playing a role in osteoporosis therapy. In this study, the structures of the human PTH fragments (1-34) and (1-39) as well as bovine PTH(1-37) in aqueous buffer solution under near physiological conditions were determined using two-dimensional nuclear magnetic resonance spectroscopy. The overall structure of the first 34 amino acids of these three peptides is virtually identical, exhibiting a short NH(2)-terminal and a longer COOH-terminal helix as well as a defined loop region from His14 to Ser17, stabilized by hydrophobic interactions. bPTH(1-37), which has a higher biological activity, shows a better-defined NH(2)-terminal part. In contrast to NH(2)-terminal truncations, which cause destabilization of helical structure, neither COOH-terminal truncation nor elongation significantly influences the secondary structure. Furthermore, we investigated the structure of hPTH(1-34) in 20% trifluoroethanol solution. In addition to its helix-stabilizing effect, trifluorethanol causes the loss of tertiary hydrophobic interactions.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20979597 M.Abraham-Nordling, B.Persson, and E.Nordling (2010).
Model of the complex of Parathyroid hormone-2 receptor and Tuberoinfundibular peptide of 39 residues.
  BMC Res Notes, 3, 270.  
19674967 A.A.Pioszak, N.R.Parker, T.J.Gardella, and H.E.Xu (2009).
Structural basis for parathyroid hormone-related protein binding to the parathyroid hormone receptor and design of conformation-selective peptides.
  J Biol Chem, 284, 28382-28391.
PDB code: 3h3g
19446460 C.Parthier, S.Reedtz-Runge, R.Rudolph, and M.T.Stubbs (2009).
Passing the baton in class B GPCRs: peptide hormone activation via helix induction?
  Trends Biochem Sci, 34, 303-310.  
17286517 E.Arashiro, J.R.Drugowich de Felício, and U.H.Hansmann (2007).
Short-time dynamics of polypeptides.
  J Chem Phys, 126, 045107.  
16711779 E.Arashiro, J.R.Drugowich de Felício, and U.H.Hansmann (2006).
Short-time dynamics of the helix-coil transition in polypeptides.
  Phys Rev E Stat Nonlin Soft Matter Phys, 73, 040902.  
15686531 A.Barazza, A.Wittelsberger, N.Fiori, E.Schievano, S.Mammi, C.Toniolo, J.M.Alexander, M.Rosenblatt, E.Peggion, and M.Chorev (2005).
Bioactive N-terminal undecapeptides derived from parathyroid hormone: the role of alpha-helicity.
  J Pept Res, 65, 23-35.  
15267304 U.H.Hansmann (2004).
Generalized-ensemble simulations of the human parathyroid hormone fragment PTH(1-34).
  J Chem Phys, 120, 417-422.  
14648764 E.Schievano, S.Mammi, E.Carretta, N.Fiori, M.Corich, A.Bisello, M.Rosenblatt, M.Chorev, and E.Peggion (2003).
Conformational and biological characterization of human parathyroid hormone hPTH(1-34) analogues containing beta-amino acid residues in positions 17-19.
  Biopolymers, 70, 534-547.  
11397646 T.J.Gardella, and H.Jüppner (2001).
Molecular properties of the PTH/PTHrP receptor.
  Trends Endocrinol Metab, 12, 210-217.  
11087406 J.R.Barbier, S.MacLean, P.Morley, J.F.Whitfield, and G.E.Willick (2000).
Structure and activities of constrained analogues of human parathyroid hormone and parathyroid hormone-related peptide: implications for receptor-activating conformations of the hormones.
  Biochemistry, 39, 14522-14530.  
11041841 Z.Chen, P.Xu, J.R.Barbier, G.Willick, and F.Ni (2000).
Solution structure of the osteogenic 1-31 fragment of the human parathyroid hormone.
  Biochemistry, 39, 12766-12777.
PDB code: 1fvy
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