Structure and function of the N-terminal domain of the human mitochondrial calcium uniporter

EMBO Reports

Volumn 16, Issue 10, 2015, Pages 1318-1333

  Lee, Youngjin ^a   Min, Choon Kee ^a,d   Kim, Tae Gyun ^a   Song, Hong Ki ^a   Lim, Yunki ^a   Kim, Dongwook ^a   Shin, Kahee ^a   Kang, Moonkyung ^b   Kang, Jung Youn ^a   Youn, Hyung Seop ^a   Lee, Jung Gyu ^a   An, Jun Yop ^a   Park, Kyoung Ryoung ^a   Lim, Jia Jia ^a   Kim, Ji Hun ^a   Kim, Ji Hye ^a   Park, Zee Yong ^a   Kim, Yeon Soo ^b   Wang, Jimin ^a,c   Kim, Do Han ^a   Eom, Soo Hyun ^a   more..

^a Gwangju Institute of Science and Technology (GIST)   (South Korea)

^b Chungnam National University   (South Korea)

^c YALE UNIVERSITY   (United States)

^d Daegu Gyeongbuk Medical Innovation Foundation   (South Korea)

Author keywords

crystal structure; MCU; MCU domain like fold; mitochondrial calcium uptake; uniplex

Indexed keywords

MITOCHONDRIAL CALCIUM UNIPORTER; MITOCHONDRIAL CALCIUM UPTAKE 1 PROTEIN; MITOCHONDRIAL CALCIUM UPTAKE 2 PROTEIN; REGULATOR PROTEIN; UNCLASSIFIED DRUG; CALCIUM; CALCIUM BINDING PROTEIN; CALCIUM CHANNEL; CARRIER PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; BIOCHEMISTRY; CALCIUM TRANSPORT; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DELETION MUTANT; FEMALE; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; CHEMISTRY; GENETICS; HEK293 CELL LINE; HELA CELL LINE; METABOLISM; MITOCHONDRION; MOLECULAR MODEL; MUTATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

CALCIUM; CALCIUM CHANNELS; CALCIUM-BINDING PROTEINS; CRYSTALLOGRAPHY, X-RAY; HEK293 CELLS; HELA CELLS; HUMANS; MITOCHONDRIA; MITOCHONDRIAL MEMBRANE TRANSPORT PROTEINS; MODELS, MOLECULAR; MUTATION; PROTEIN FOLDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 84942776229     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.15252/embr.201540436     Document Type: Article

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