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PDBsum entry 3k2s

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protein ligands Protein-protein interface(s) links
Lipid binding protein PDB id
3k2s
Jmol
Contents
Protein chains
243 a.a. *
Ligands
POV ×200
CLR ×20
* Residue conservation analysis
PDB id:
3k2s
Name: Lipid binding protein
Title: Solution structure of double super helix model
Structure: Apolipoprotein a-i. Chain: a, b. Synonym: apo-ai, apoa-i, apolipoprotein a-i(1-242). Engineered: yes
Source: Homo sapiens. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Authors: Z.Wu,V.Gogonea,X.Lee,M.A.Wagner,X.-M.Li,Y.Huang,A.Undurti,R. M.Haertlein,M.Moulin,I.Gutsche,G.Zaccai,J.A.Didonato,L.S.Ha
Key ref: Z.Wu et al. (2009). Double superhelix model of high density lipoprotein. J Biol Chem, 284, 36605-36619. PubMed id: 19812036
Date:
30-Sep-09     Release date:   07-Apr-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

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

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   19 terms 
  Biological process     small molecule metabolic process   67 terms 
  Biochemical function     chemorepellent activity     18 terms  

 

 
J Biol Chem 284:36605-36619 (2009)
PubMed id: 19812036  
 
 
Double superhelix model of high density lipoprotein.
Z.Wu, V.Gogonea, X.Lee, M.A.Wagner, X.M.Li, Y.Huang, A.Undurti, R.P.May, M.Haertlein, M.Moulin, I.Gutsche, G.Zaccai, J.A.Didonato, S.L.Hazen.
 
  ABSTRACT  
 
High density lipoprotein (HDL), the carrier of so-called "good" cholesterol, serves as the major athero-protective lipoprotein and has emerged as a key therapeutic target for cardiovascular disease. We applied small angle neutron scattering (SANS) with contrast variation and selective isotopic deuteration to the study of nascent HDL to obtain the low resolution structure in solution of the overall time-averaged conformation of apolipoprotein AI (apoA-I) versus the lipid (acyl chain) core of the particle. Remarkably, apoA-I is observed to possess an open helical shape that wraps around a central ellipsoidal lipid phase. Using the low resolution SANS shapes of the protein and lipid core as scaffolding, an all-atom computational model for the protein and lipid components of nascent HDL was developed by integrating complementary structural data from hydrogen/deuterium exchange mass spectrometry and previously published constraints from multiple biophysical techniques. Both SANS data and the new computational model, the double superhelix model, suggest an unexpected structural arrangement of protein and lipids of nascent HDL, an anti-parallel double superhelix wrapped around an ellipsoidal lipid phase. The protein and lipid organization in nascent HDL envisages a potential generalized mechanism for lipoprotein biogenesis and remodeling, biological processes critical to sterol and lipid transport, organismal energy metabolism, and innate immunity.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21399642 R.Huang, R.A.Silva, W.G.Jerome, A.Kontush, M.J.Chapman, L.K.Curtiss, T.J.Hodges, and W.S.Davidson (2011).
Apolipoprotein A-I structural organization in high-density lipoproteins isolated from human plasma.
  Nat Struct Mol Biol, 18, 416-422.  
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