PDBsum entry 1anp

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Hypotensive hormone PDB id
Protein chain
28 a.a.*
* C-alpha coords only
PDB id:
Name: Hypotensive hormone
Title: Solution conformation of an atrial natriuretic peptide variant selective for the type-a receptor
Structure: Atrial natriuretic peptide. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: potential
NMR struc: 11 models
Authors: W.J.Fairbrother,R.S.Mcdowell,B.C.Cunningham
Key ref:
W.J.Fairbrother et al. (1994). Solution conformation of an atrial natriuretic peptide variant selective for the type A receptor. Biochemistry, 33, 8897-8904. PubMed id: 8043577 DOI: 10.1021/bi00196a006
06-Apr-94     Release date:   07-Apr-95    

Protein chain
Pfam   ArchSchema ?
P01160  (ANF_HUMAN) -  Natriuretic peptides A
153 a.a.
28 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 6 residue positions (black crosses)


    Key reference    
DOI no: 10.1021/bi00196a006 Biochemistry 33:8897-8904 (1994)
PubMed id: 8043577  
Solution conformation of an atrial natriuretic peptide variant selective for the type A receptor.
W.J.Fairbrother, R.S.McDowell, B.C.Cunningham.
Two-dimensional NMR spectroscopy has been used to characterize the solution conformation of an atrial natriuretic peptide (ANP) variant which is selective for the human natriuretic peptide receptor A (NPR-A) relative to receptor C (NPR-C). The ANP mutant, containing six substitutions, has reduced flexibility in aqueous solution relative to wild-type ANP and allows the observation of sufficient NOE connectivities for structure determination by distance geometry and restrained molecular dynamics calculations. The solution conformation is reasonably well defined, having an average backbone atom rms deviation from the average coordinates of approximately 1.1 A for residues 7-27. The structure is consistent with available functional data and shows a spatial separation between known receptor binding determinants and residues found to be outside the hormone-receptor interface.

Literature references that cite this PDB file's key reference

  PubMed id Reference
18470479 E.Malito, R.E.Hulse, and W.J.Tang (2008).
Amyloid beta-degrading cryptidases: insulin degrading enzyme, presequence peptidase, and neprilysin.
  Cell Mol Life Sci, 65, 2574-2585.  
16650056 O.K.Baryshnikova, J.K.Rainey, and B.D.Sykes (2005).
Nuclear magnetic resonance studies of CXC chemokine receptor 4 allosteric peptide agonists in solution.
  J Pept Res, 66, 12-21.  
11839490 H.J.Dyson, and P.E.Wright (2002).
Coupling of folding and binding for unstructured proteins.
  Curr Opin Struct Biol, 12, 54-60.  
11533490 He Xl, Chow Dc, M.M.Martick, and K.C.Garcia (2001).
Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone.
  Science, 293, 1657-1662.
PDB codes: 1jdn 1jdp
9790687 R.E.Hileman, R.N.Jennings, and R.J.Linhardt (1998).
Thermodynamic analysis of the heparin interaction with a basic cyclic peptide using isothermal titration calorimetry.
  Biochemistry, 37, 15231-15237.  
9209157 K.A.Carpenter, B.C.Wilkes, A.De Léan, A.Fournier, and P.W.Schiller (1997).
Hydrophobic forces are responsible for the folding of a highly potent natriuretic peptide analogue at a membrane mimetic surface: an NMR study.
  Biopolymers, 42, 37-48.  
9261088 P.A.Carr, H.P.Erickson, and A.G.Palmer (1997).
Backbone dynamics of homologous fibronectin type III cell adhesion domains from fibronectin and tenascin.
  Structure, 5, 949-959.  
8841141 N.McNicoll, J.Gagnon, J.J.Rondeau, H.Ong, and A.De Léan (1996).
Localization by photoaffinity labeling of natriuretic peptide receptor-A binding domain.
  Biochemistry, 35, 12950-12956.  
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 codes are shown on the right.