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PDBsum entry 1hph

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protein links
Hormone PDB id
1hph
Jmol
Contents
Protein chain
37 a.a. *
* Residue conservation analysis
PDB id:
1hph
Name: Hormone
Title: Structure of human parathyroid hormone 1-37 in solution
Structure: Human parathyroid hormone fragment 1 - 37. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606
NMR struc: 10 models
Authors: U.C.Marx,P.Roesch
Key ref: U.C.Marx et al. (1995). Structure of human parathyroid hormone 1-37 in solution. J Biol Chem, 270, 15194-15202. PubMed id: 7797503
Date:
14-Feb-95     Release date:   10-Jul-95    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01270  (PTHY_HUMAN) -  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  

 

 
J Biol Chem 270:15194-15202 (1995)
PubMed id: 7797503  
 
 
Structure of human parathyroid hormone 1-37 in solution.
U.C.Marx, S.Austermann, P.Bayer, K.Adermann, A.Ejchart, H.Sticht, S.Walter, F.X.Schmid, R.Jaenicke, W.G.Forssmann.
 
  ABSTRACT  
 
Human parathyroid hormone (hPTH), amino acids Ser1 to Leu37, is biologically active with respect to both receptor binding and activation of adenylate cyclase to influence the serum calcium concentration. It induces DNA synthesis via an unknown signal pathway. We investigated the structure of hPTH(1-37) in H2O/buffer solution under near physiological conditions, that is pH 6.0 and 270 mM salt, by circular dichroism, ultracentrifugation, nuclear magnetic resonance spectroscopy, and molecular dynamics calculations. Complete sequence specific assignments of all 1H resonances were performed by using 1H two-dimensional NMR measurements (double quantum-filtered correlated spectroscopy, nuclear Overhauser effect spectroscopy (NOESY), and total correlation spectroscopy with suppression of NOESY-type cross-peaks spectra). hPTH(1-37) obtained helical structure and showed hydrophobic interactions defining a tertiary structure. The NH2-terminal four amino acids of hPTH(1-37) did not show a stable conformation. Evidence for an alpha-helical region between Ile5 and Asn10 was found. This region was followed by a flexible link (Gly12, Lys13) and a well defined turn region, His14 to Ser17. The latter was stabilized by hydrophobic interactions between Trp23 and Leu15. Ser17 through at least Leu28 formed an alpha-helix. Arg20 and Lys27 were involved in the core built by His14 to Ser17. Unrestrained molecular dynamics simulations indicated that the structure was stable on the 200 ps time scale.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18375760 A.A.Pioszak, and H.E.Xu (2008).
Molecular recognition of parathyroid hormone by its G protein-coupled receptor.
  Proc Natl Acad Sci U S A, 105, 5034-5039.
PDB code: 3c4m
17525467 T.J.Kamerzell, S.B.Joshi, D.McClean, L.Peplinskie, K.Toney, D.Papac, M.Li, and C.R.Middaugh (2007).
Parathyroid hormone is a heparin/polyanion binding protein: binding energetics and structure modification.
  Protein Sci, 16, 1193-1203.  
16123988 M.Scian, M.Marin, M.Bellanda, L.Tou, J.M.Alexander, M.Rosenblatt, M.Chorev, E.Peggion, and S.Mammi (2006).
Backbone dynamics of human parathyroid hormone (1-34): flexibility of the central region under different environmental conditions.
  Biopolymers, 84, 147-160.  
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.  
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.  
12383114 J.Jung, S.K.Lim, Y.Kim, and W.Lee (2002).
NMR structure of a minimum activity domain of human parathyroid peptide hormone: structural origin of receptor activation.
  J Pept Res, 60, 239-246.  
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.  
9265617 D.F.Mierke, S.Maretto, E.Schievano, D.DeLuca, A.Bisello, S.Mammi, M.Rosenblatt, E.Peggion, and M.Chorev (1997).
Conformational studies of mono- and bicyclic parathyroid hormone-related protein-derived agonists.
  Biochemistry, 36, 10372-10383.  
9108685 D.Klostermeier, P.Bayer, M.Kraft, R.W.Frank, and P.Rösch (1997).
Spectroscopic investigations of HIV-1 trans-activator and related peptides in aqueous solutions.
  Biophys Chem, 63, 87-96.  
9182993 D.Willbold, S.Hoffmann, and P.Rösch (1997).
Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution.
  Eur J Biochem, 245, 581-588.
PDB code: 1vpu
9395339 K.Kanaori, M.Takai, and A.Y.Nosaka (1997).
Comparative study of chicken and human parathyroid hormone-(1-34)-peptides in solution with SDS.
  Eur J Biochem, 249, 878-885.  
  9461349 W.Gronwald, D.Schomburg, W.Tegge, and V.Wray (1997).
Assessment by 1H NMR spectroscopy of the structural behaviour of human parathyroid-hormone-related protein(1-34) and its close relationship with the N-terminal fragments of human parathyroid hormone in solution.
  Biol Chem, 378, 1501-1508.  
8647119 H.Sticht, G.Wildegger, D.Bentrop, B.Darimont, R.Sterner, and P.Rösch (1996).
An NMR-derived model for the solution structure of oxidized Thermotoga maritima 1[Fe4-S4] ferredoxin.
  Eur J Biochem, 237, 726-735.
PDB code: 1rof
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.