TABLE 1

Hydrogen bond (H) and salt bridge (SB) interactions between a peptide and the helical cavity from the available crystal structures of class A GPCRs bound to a peptide

PeptideReceptorOverall Number of ContactsNumber of Contacts with Peptide Side ChainsNumber of Contacts with Peptide BackboneNumber of Contacts with Peptide Terminal GroupNumber of Peptide Residues within the CavityPDB Code
ApelinAPLNR82H+1SBa2H2H+1SB65VBL
NeurotensinNTS161H1H3H+1SB44GRV
EndothelinETB164H+1SB6H3H+2SB165GLH
[Sar1, Ile8]AngIIAT2123H+1SB6H1H+1SB65XJM
DIPP-NH2DOR41H2H+1SB34RWD
DAMGOMOR41H2H+1SB56DDF
CX3CL1US2851H3H1H74XT3
CX3CL1/Nb7US2872H4H1H114XT1
vMIP-IICXCR4136H+2SB2H2H+1SB94RWS
CVX15CXCR4106H+3SB1H63OE0
cyclicPMX53C5a1126H+1SB5H36C1R
  • a Hydrogen bond criteria: 3 Å for the maximum distance between donor and acceptor atoms, 90° and 60° for donor and acceptor minimum angles, respectively. Salt bridge criteria: the maximum distance between atoms is 5 Å.