Structural study of caveolin-1 intramembrane domain by CD and NMR.
 

Structural study of caveolin-1 intramembrane domain by CD and NMR.

http://www.bionmr.com//www.ncbi.nlm....x_FullText.gif Related Articles Structural study of caveolin-1 intramembrane domain by CD and NMR.

Biopolymers. 2014 Dec 4;

Authors: Yang G, Dong Z, Xu H, Wang C, Li H, Li Z, Li F

Abstract
Caveolin-1 is a main structural component of caveolae and essential for the invagination of caveolae by forming a hairpin structure in the membrane-inserting domain (residues 102-122). In the present paper, we determined the tertiary structures of the peptides comprising residues 93-126 and 101-126 of caveolin-1in 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP) aqueous solution and sodium dodecyl sulfate (SDS) micelles, respectively, by NMR study. The self-association of the peptides in SDS and dodecylphosphocholine (DPC) micelles was also studied by CD, NMR and SDS-PAGE techniques. Our results indicated that both peptides form a helix-break-helix structure with two helices spanning over Leu103-Phe107 and Ile117-His126 and a loop ranging over Gly108-Gly116. The addition of the segment Thr93-Arg101 to the N-terminal end of the intramembrane domain promoted more oligomerization of the peptide 93-126 than the peptide 101-126 in the micelles. Our results suggested that the glycine residues at position 108 and 116 are important for the break of the helical structure of the membrane-inserting domain and the segment Thr93-Arg101 flanking the membrane-inserting domain may play a role in the self-association of the caveolin-1 protein at cellular membrane. This article is protected by copyright. All rights reserved.


PMID: 25471446 [PubMed - as supplied by publisher]



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