Crystal structure of the human NK1 tachykinin receptor

Yin, Jie; Chapman, Karen; Clark, Lindsay D.; Shao, Zhenhua; Borek, Dominika; Xu, Qingping; Wang, Junmei; Rosenbaum, Daniel M.

doi:10.1073/pnas.1812717115

Title: Crystal structure of the human NK₁ tachykinin receptor

Journal Article · Tue Dec 11 00:00:00 EST 2018 · Proceedings of the National Academy of Sciences of the United States of America

DOI:https://doi.org/10.1073/pnas.1812717115· OSTI ID:1493430

Yin, Jie ^[1]; Chapman, Karen ^[1]; Clark, Lindsay D. ^[1]; Shao, Zhenhua ^[1];

^[1]; Xu, Qingping ^[2]; Wang, Junmei ^[3];

^[1]

The Univ. of Texas Southwest Medical Center, Dallas, TX (United States)
Argonne National Lab. (ANL), Argonne, IL (United States)
Univ. of Pittsburgh, Pittsburgh, PA (United States)

The NK₁ tachykinin G-protein–coupled receptor (GPCR) binds substance P, the first neuropeptide to be discovered in mammals. Through activation of NK₁R, substance P modulates a wide variety of physiological and disease processes including nociception, inflammation, and depression. Human NK₁R (hNK₁R) modulators have shown promise in clinical trials for migraine, depression, and emesis. However, the only currently approved drugs targeting hNK₁R are inhibitors for chemotherapy-induced nausea and vomiting (CINV). To better understand the molecular basis of ligand recognition and selectivity, we solved the crystal structure of hNK₁R bound to the inhibitor L760735, a close analog of the drug aprepitant. Our crystal structure reveals the basis for antagonist interaction in the deep and narrow orthosteric pocket of the receptor. We used our structure as a template for computational docking and molecular-dynamics simulations to dissect the energetic importance of binding pocket interactions and model the binding of aprepitant. Furthermore, the structure of hNK₁R is a valuable tool in the further development of tachykinin receptor modulators for multiple clinical applications.

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Research Organization:: Argonne National Lab. (ANL), Argonne, IL (United States)

Sponsoring Organization:: Welch Foundation; National Institutes of Health (NIH); USDOE

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1493430

Journal Information:: Proceedings of the National Academy of Sciences of the United States of America, Vol. 115, Issue 52; ISSN 0027-8424

Publisher:: National Academy of Sciences, Washington, DC (United States)Copyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 20 works

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