PDBsum entry 1zwc

Go to PDB code: 
protein links
Hormone PDB id
Protein chain
37 a.a. *
* Residue conservation analysis
PDB id:
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
17-Jun-96     Release date:   12-Mar-97    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P01268  (PTHY_BOVIN) -  Parathyroid hormone
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.
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
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.