Crystal structure of a multi-domain human smoothened receptor in complex with a super stabilizing ligand

Nature Communications

Volumn 8, Issue , 2017, Pages

  Zhang, Xianjun ^a,b,c   Zhao, Fei ^a   Wu, Yiran ^a   Yang, Jun ^d   Han, Gye Won ^e   Zhao, Suwen ^a   Ishchenko, Andrii ^e   Ye, Lintao ^a,f   Lin, Xi ^a,b,c   Ding, Kang ^a,c   Dharmarajan, Venkatasubramanian ^g   Griffin, Patrick R ^g   Gati, Cornelius ^h   Nelson, Garrett ⁱ   Hunter, Mark S ^j   Hanson, Michael A ^k   Cherezov, Vadim ^e   Stevens, Raymond C ^a   Tan, Wenfu ^d   Tao, Houchao ^a   Xu, Fei ^a   more..

^a SHANGHAITECH UNIVERSITY   (China)

^b INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

^c UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

^d FUDAN UNIVERSITY   (China)

^e UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

^f SHANGHAI INSTITUTE OF MATERIA MEDICA   (China)

^g SCRIPPS RESEARCH INSTITUTE   (United States)

^h MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

ⁱ ARIZONA STATE UNIVERSITY   (United States)

^j SLAC NATIONAL ACCELERATOR LABORATORY   (United States)

^k GPCR Consortium   (United States)

more..

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; SMOOTHENED PROTEIN; LIGAND; PROTEIN BINDING; RECOMBINANT PROTEIN; SMO PROTEIN, HUMAN; SONIC HEDGEHOG PROTEIN;

AMINO ACID; CRYSTAL STRUCTURE; DEUTERIUM; HYDROGEN; LASER; LIGAND; SIMULATION;

ALLOSTERISM; ARTICLE; CRYSTAL STRUCTURE; DEUTERIUM HYDROGEN EXCHANGE; MOLECULAR DYNAMICS; BINDING SITE; CHEMISTRY; HEK293 CELL LINE; HUMAN; ISOLATION AND PURIFICATION; MASS SPECTROMETRY; METABOLISM; PROCEDURES; PROTEIN DOMAIN; SIGNAL TRANSDUCTION; X RAY CRYSTALLOGRAPHY;

ERINACEIDAE;

BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DEUTERIUM EXCHANGE MEASUREMENT; HEDGEHOG PROTEINS; HEK293 CELLS; HUMANS; LIGANDS; MASS SPECTROMETRY; MOLECULAR DYNAMICS SIMULATION; PROTEIN BINDING; PROTEIN DOMAINS; RECOMBINANT PROTEINS; SIGNAL TRANSDUCTION; SMOOTHENED RECEPTOR;

EID: 85019947839     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms15383     Document Type: Article

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