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Structural biology of human cannabinoid receptor-2 helix 6 in membrane-mimetic environments.

Tiburu EK, Tyukhtenko S, Deshmukh L, Vinogradova O, Janero DR, Makriyannis A
Biochem Biophys Res Commun 384 243-8 (2009)
Cited: 12 times
EuropePMC logo PMID: 19397896

Abstract

We detail the structure and dynamics of a synthetic peptide corresponding to transmembrane helix 6 (TMH6) of human cannabinoid receptor-2 (hCB2) in biomembrane-mimetic environments. The peptide's NMR structural biology is characterized by two alpha-helical domains bridged by a flexible, nonhelical hinge region containing a highly-conserved CWFP motif with an environmentally sensitive, Pro-based conformational switch. Buried within the peptide's flexible region, W(258) may hydrogen-bond with L(255) to help stabilize the Pro-kinked hCB2 TMH6 structure and position C(257) advantageously for interaction with agonist ligands. These characteristics of hCB2 TMH6 are potential structural features of ligand-induced hCB2 activation in vivo.

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  1. Selective Targeting of Lung Cancer Cells with Methylparaben-Tethered-Quinidine Cocrystals in 3D Spheroid Models. Krishnamoorthi S, Kasinathan GN, Paramasivam G, Rath SN, Prakash J. ACS Omega 8 46628-46639 (2023)


Reviews citing this publication (2)

  1. Challenges and Perspectives in Chemical Synthesis of Highly Hydrophobic Peptides. Mueller LK, Baumruck AC, Zhdanova H, Tietze AA. Front Bioeng Biotechnol 8 162 (2020)
  2. Invited review: GPCR structural characterization: Using fragments as building blocks to determine a complete structure. Cohen LS, Fracchiolla KE, Becker J, Naider F. Biopolymers 102 223-243 (2014)

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