Two-site binding of C5a by its receptor: analternative binding paradigm for G protein-coupled receptors. | Zendy

Salvatore Siciliano | Zendy; Thomas E. Rollins | Zendy; Julie A. DeMartino | Zendy; Ze Konteatis | Zendy; Lorraine Malkowitz | Zendy; Gail Van Riper | Zendy; Steven Bondy | Zendy; Hugh Rosen | Zendy; Martin S. Springer | Zendy

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Two-site binding of C5a by its receptor: analternative binding paradigm for G protein-coupled receptors.

Author(s) -

Salvatore Siciliano,

Thomas E. Rollins,

Julie A. DeMartino,

Ze Konteatis,

Lorraine Malkowitz,

Gail Van Riper,

Steven Bondy,

Hugh Rosen,

Martin S. Springer

Publication year - 1994

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.91.4.1214

Subject(s) - receptor , c5a receptor , binding site , biochemistry , g protein coupled receptor , biology , plasma protein binding , structural motif , chemistry , genetics , complement system , antibody

The guanine nucleotide-binding protein-coupledreceptor superfamily binds a vast array of biological messengers includinglipids, odorants, catecholamines, peptides, and proteins. While some smallmolecules bind to these receptors at a single interhelical site, we find thatthe binding domain on the receptor for the inflammatory protein C5a is morecomplex and consists of two distinct subsites. This more elaborate motif appearsto be an evolutionary adaptation of the simpler paradigm to which a secondinteraction site has been added in the receptor N terminus. Surprisingly,occupation of only one of the subsites is required for receptor activation. Thetwo-site motif is not unique to the C5a receptor but appears to be widely usedby the superfamily to accommodate macromolecular ligands.

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