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Summary Structural Experimental Function Sequence Neighbor Download Link


<Asymmetric unit>

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PDB ID1gw3  sequence information (FASTA format)   
DescriptorAPOA-I
TitleTHE HELIX-HINGE-HELIX STRUCTURAL MOTIF IN HUMAN APOLIPOPROTEIN A-I DETERMINED BY NMR SPECTROSCOPY, 1 STRUCTURE
Functional KeywordsHIGH DENSITY LIPOPROTEINS, KEY IN VIVO COFACTOR FOR THE ENZYME LECITHIN-CHOLESTEROL TRANSFERASE, CHOLESTEROL EFFLUX, RECEPTOR BINDING, AMPHIPATHIC HELICES, HELIX-HINGE-HELIX MOTIF
Biological sourceHomo sapiens (human)
Cellular location [UNP - P02647] Secreted
Organ source [UNP - P02647] Brain, and Skeletal muscle
[UNP - P02647] Heart
[UNP - P02647] Platelet
[UNP - P02647] Brain, Cajal-Retzius cell, and Fetal brain cortex
Total number of polymer chains1
Total molecular weight5151.8 (the details in Structural Details Page)
AuthorsWang, G. , Sparrow, J.T. , Cushley, R.J. (deposition date : 1997-06-04, release date : 1997-07-23)
Primary citationWang, G. , Sparrow, J.T. , Cushley, R.J.
The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR spectroscopy.
Biochemistry, 36:13657 - 13666, 1997.(PubMed : 9354635)  (DOI: 10.1021/bi971151q)
Experimental methodSOLUTION NMR
Other Database Information
Yorodumi , CATH , CE , FSSP , SCOP , VAST , UniProt ( P02647 ) , eF-site , PISA , NRG-CING