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PDBsum entry 1bzg

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protein links
Hormone PDB id
1bzg
Jmol
Contents
Protein chain
34 a.a. *
* Residue conservation analysis
PDB id:
1bzg
Name: Hormone
Title: The solution structure of human parathyroid hormone-related protein (1-34) in near-physiological solution, nmr, 30 structures
Structure: Parathyroid hormone-related protein. Chain: a. Fragment: residues 1-34. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606
NMR struc: 30 models
Authors: M.Weidler,U.C.Marx,G.Seidel,P.Roesch
Key ref:
M.Weidler et al. (1999). The structure of human parathyroid hormone-related protein(1-34) in near-physiological solution. FEBS Lett, 444, 239-244. PubMed id: 10050767 DOI: 10.1016/S0014-5793(98)01658-5
Date:
28-Oct-98     Release date:   18-May-99    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P12272  (PTHR_HUMAN) -  Parathyroid hormone-related protein
Seq:
Struc:
177 a.a.
34 a.a.
Key:    PfamA domain  Secondary structure

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biological process     regulation of chondrocyte differentiation   1 term 
  Biochemical function     hormone activity     1 term  

 

 
DOI no: 10.1016/S0014-5793(98)01658-5 FEBS Lett 444:239-244 (1999)
PubMed id: 10050767  
 
 
The structure of human parathyroid hormone-related protein(1-34) in near-physiological solution.
M.Weidler, U.C.Marx, G.Seidel, W.Schäfer, E.Hoffmann, A.Esswein, P.Rösch.
 
  ABSTRACT  
 
Parathyroid hormone-related protein plays a major role in the pathogenesis of humoral hypercalcemia of malignancy. Under normal physiological conditions, parathyroid hormone-related protein is produced in a wide variety of tissues and acts in an autocrine or paracrine fashion. Parathyroid hormone-related protein and parathyroid hormone bind to and activate the same G-protein-coupled receptor. Here we present the structure of the biologically active NH2-terminal domain of human parathyroid hormone-related protein(1-34) in near-physiological solution in the absence of crowding reagents as determined by two-dimensional proton magnetic resonance spectroscopy. An improved strategy for structure calculation revealed the presence of two helices, His-5-Leu-8 and Gln-16-Leu-27, connected by a flexible linker. The parathyroid hormone-related protein(1-34) structure and the structure of human parathyroid hormone(1-37) as well as human parathyroid hormone(1-34) are highly similar, except for the well defined turn, His-14-Ser-17, present in parathyroid hormone. Thus, the similarity of the binding affinities of parathyroid hormone and parathyroid hormone-related protein to their common receptor may be based on their structural similarity.
 
  Selected figure(s)  
 
Figure 1.
Fig. 1. CD spectrum of hPTHrP(1â34) at 298 K, 1 mg/ml ( vert, similar 250 μM) peptide in 50 mM potassium phosphate, pH 5.1, 250 mM sodium chloride.
Figure 4.
Fig. 4. MOLMOL 2.5.1 [47] cartoon of the lowest internal energy structure. The amino- and carboxy-termini are indicated.
 
  The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (1999, 444, 239-244) copyright 1999.  
  Figures were selected by an automated process.  

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
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.  
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.  
12080067 M.Shimada, X.Chen, T.Cvrk, H.Hilfiker, M.Parfenova, and G.V.Segre (2002).
Purification and characterization of a receptor for human parathyroid hormone and parathyroid hormone-related peptide.
  J Biol Chem, 277, 31774-31780.  
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.  
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.