Structural and functional characterization of the JH2 pseudokinase domain of JAK family tyrosine kinase 2 (TYK2)

Journal of Biological Chemistry

Volumn 290, Issue 45, 2015, Pages 27261-27270

  Min, Xiaoshan ^a   Ungureanu, Daniela ^b   Maxwell, Sarah ^a   Hammarén, Henrik ^b   Thibault, Steve ^a   Hillert, Ellin Kristina ^c   Ayres, Merrill ^a   Greenfield, Brad ^a   Eksterowicz, John ^a   Gabel, Chris ^a   Walker, Nigel ^a   Silvennoinen, Olli ^b,c   Wang, Zhulun ^a  

^a AMGEN INC   (United States)

^b TAMPERE UNIVERSITY OF TECHNOLOGY   (Finland)

^c TAMPERE UNIVERSITY HOSPITAL   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS;

ACTIVATION LOOPS; ATP BINDING; ENZYMATIC ACTIVITIES; FUNCTIONAL CHARACTERIZATION; PSEUDOKINASE; REGULATORY FUNCTIONS; TYROSINE KINASE;

BINS;

ADENOSINE 5' O (THIOTRIPHOSPHATE); ADENOSINE DERIVATIVE; ADENOSINE TRIPHOSPHATE; JANUS KINASE; TYROSINE KINASE 2; UNCLASSIFIED DRUG; JAK1 PROTEIN, HUMAN; JAK2 PROTEIN, HUMAN; JANUS KINASE 1; JANUS KINASE 2; PROTEIN KINASE TYK2; TYK2 PROTEIN, HUMAN;

ARTICLE; CATALYSIS; COMPARATIVE STUDY; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME PHOSPHORYLATION; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; JH2 PSEUDOKINASE DOMAIN; PRIORITY JOURNAL; PROTEIN FUNCTION; STRUCTURE ANALYSIS; AMINO ACID SEQUENCE; CHEMISTRY; ENZYME ACTIVATION; ENZYME STABILITY; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; MOLECULAR MODEL; MUTATION; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; STRUCTURAL HOMOLOGY; X RAY CRYSTALLOGRAPHY;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; ENZYME STABILITY; HUMANS; JANUS KINASE 1; JANUS KINASE 2; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURAL HOMOLOGY, PROTEIN; TYK2 KINASE;

EID: 84946738706     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.672048     Document Type: Article

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