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PDBsum entry 1gw3

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protein links
High density lipoproteins PDB id
1gw3
Jmol
Contents
Protein chain
46 a.a. *
* Residue conservation analysis
PDB id:
1gw3
Name: High density lipoproteins
Title: The helix-hinge-helix structural motif in human apolipoprotein a-i determined by nmr spectroscopy, 1 structure
Structure: Apoa-i. Chain: a. Fragment: residues 142 - 187. Synonym: apolipoprotein a-i. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606
NMR struc: 1 models
Authors: G.Wang,J.T.Sparrow,R.J.Cushley
Key ref:
G.Wang et al. (1997). The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR spectroscopy. Biochemistry, 36, 13657-13666. PubMed id: 9354635 DOI: 10.1021/bi971151q
Date:
04-Jun-97     Release date:   23-Jul-97    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P02647  (APOA1_HUMAN) -  Apolipoprotein A-I
Seq:
Struc:
267 a.a.
46 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1021/bi971151q Biochemistry 36:13657-13666 (1997)
PubMed id: 9354635  
 
 
The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR spectroscopy.
G.Wang, J.T.Sparrow, R.J.Cushley.
 
  ABSTRACT  
 
The conformation of a synthetic peptide of 46 residues from apoA-I was investigated by fluorescence, CD, and 2D NMR spectroscopies in lipid-mimetic environments. ApoA-I(142-187) is mainly unstructured in water but helical in SDS or dodecylphosphocholine (DPC), although the peptide only associates with DPC at approximately the critical micellar concentration. Solution structures of apoA-I(142-187) were determined by distance geometry calculations based on 450 (in DPC-d38) or 397 (in SDS-d25) NOE-derived distance restraints, respectively. Backbone RMSDs for superimposing the two helical regions 146-162 and 168-182 are 0.98 +/- 0.22 (2.38 +/- 0.20) and 1.99 +/- 0.42 (2.02 +/- 0.21) A in DPC (SDS), respectively. No interhelical NOE was found, suggesting that helix-helix interactions between the two helical domains in apoA-I(142-187) are unlikely. Similar average, curved helix-hinge-helix structures were found in both SDS and DPC micelles with the hydrophobic residues occupying the concave face, indicating that hydrophobic interactions dominate. Intermolecular NOESY experiments, performed in the presence of 50% protonated SDS, confirm that the two amphipathic helices and Y166 in the hinge all interact with the micelle. The involvement of Y166 in lipid binding is supported by fluorescence spectroscopy as well. On the basis of all the data above, we propose a model for the peptide-lipid complexes wherein the curved amphipathic helix-hinge-helix structural motif straddles the micelle. The peptide-aided signal assignment achieved for apoA-I(122-187) (66mer) and apoA-I suggests that such a structural motif is retained in the longer peptide and most likely in the intact protein.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21341823 M.Beer, J.Kussmann, and C.Ochsenfeld (2011).
Nuclei-selected NMR shielding calculations: A sublinear-scaling quantum-chemical method.
  J Chem Phys, 134, 074102.  
19570799 A.Y.Shih, S.G.Sligar, and K.Schulten (2009).
Maturation of high-density lipoproteins.
  J R Soc Interface, 6, 863-871.  
17890395 F.Dancea, K.Kami, and M.Overduin (2008).
Lipid interaction networks of peripheral membrane proteins revealed by data-driven micelle docking.
  Biophys J, 94, 515-524.  
17154396 C.Beaufils, C.Alexopoulos, M.P.Petraki, A.D.Tselepis, N.Coudevylle, M.Sakarellos-Daitsiotis, C.Sakarellos, and M.T.Cung (2007).
Conformational study of new amphipathic alpha-helical peptide models of apoA-I as potential atheroprotective agents.
  Biopolymers, 88, 362-372.  
17935693 C.M.Gabrys, and D.P.Weliky (2007).
Chemical shift assignment and structural plasticity of a HIV fusion peptide derivative in dodecylphosphocholine micelles.
  Biochim Biophys Acta, 1768, 3225-3234.  
17176085 J.Song, M.S.Lee, I.Carlberg, A.V.Vener, and J.L.Markley (2006).
Micelle-induced folding of spinach thylakoid soluble phosphoprotein of 9 kDa and its functional implications.
  Biochemistry, 45, 15633-15643.
PDB code: 2fft
17107880 L.Obici, G.Franceschini, L.Calabresi, S.Giorgetti, M.Stoppini, G.Merlini, and V.Bellotti (2006).
Structure, function and amyloidogenic propensity of apolipoprotein A-I.
  Amyloid, 13, 191-205.  
15153103 E.Szolajska, J.Poznanski, M.L.Ferber, J.Michalik, E.Gout, P.Fender, I.Bailly, B.Dublet, and J.Chroboczek (2004).
Poneratoxin, a neurotoxin from ant venom. Structure and expression in insect cells and construction of a bio-insecticide.
  Eur J Biochem, 271, 2127-2136.
PDB code: 1g92
11988467 R.J.Cushley, and M.Okon (2002).
NMR studies of lipoprotein structure.
  Annu Rev Biophys Biomol Struct, 31, 177-206.  
11278170 C.G.Brouillette, G.M.Anantharamaiah, J.A.Engler, and D.W.Borhani (2001).
Structural models of human apolipoprotein A-I: a critical analysis and review.
  Biochim Biophys Acta, 1531, 4.  
11072226 X.Gao, and T.C.Wong (2001).
NMR studies of adrenocorticotropin hormone peptides in sodium dodecylsulfate and dodecylphosphocholine micelles: proline isomerism and interactions of the peptides with micelles.
  Biopolymers, 58, 20-32.  
  10975576 G.W.Buchko, A.Rozek, P.Kanda, M.A.Kennedy, and R.J.Cushley (2000).
Structural studies of a baboon (Papio sp.) plasma protein inhibitor of cholesteryl ester transferase.
  Protein Sci, 9, 1548-1558.
PDB code: 1eze
10903476 R.Storjohann, A.Rozek, J.T.Sparrow, and R.J.Cushley (2000).
Structure of a biologically active fragment of human serum apolipoprotein C-II in the presence of sodium dodecyl sulfate and dodecylphosphocholine.
  Biochim Biophys Acta, 1486, 253-264.
PDB code: 1by6
  10493581 D.Clayton, I.M.Brereton, P.A.Kroon, and R.Smith (1999).
NMR studies of the low-density lipoprotein receptor-binding peptide of apolipoprotein E bound to dodecylphosphocholine micelles.
  Protein Sci, 8, 1797-1805.  
9718294 D.P.Rogers, L.M.Roberts, J.Lebowitz, G.Datta, G.M.Anantharamaiah, J.A.Engler, and C.G.Brouillette (1998).
The lipid-free structure of apolipoprotein A-I: effects of amino-terminal deletions.
  Biochemistry, 37, 11714-11725.  
9649334 J.E.Johnson, N.M.Rao, S.W.Hui, and R.B.Cornell (1998).
Conformation and lipid binding properties of four peptides derived from the membrane-binding domain of CTP:phosphocholine cytidylyltransferase.
  Biochemistry, 37, 9509-9519.  
9753480 P.G.Frank, D.N'Guyen, V.Franklin, T.Neville, M.Desforges, E.Rassart, D.L.Sparks, and Y.L.Marcel (1998).
Importance of central alpha-helices of human apolipoprotein A-I in the maturation of high-density lipoproteins.
  Biochemistry, 37, 13902-13909.  
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.