Lipids regulate Lck protein activity through their interactions with the Lck Src homology 2 domain

Journal of Biological Chemistry

Volumn 291, Issue 34, 2016, Pages 17639-17650

  Sheng, Ren ^a   Jung, Da Jung ^b   Silkov, Antonina ^c   Kim, Hyunjin ^a   Singaram, Indira ^a   Wang, Zhi Gang ^a   Xin, Yao ^a   Kim, Eui ^b   Park, Mi Jeong ^b   Thiagarajan Rosenkranz, Pallavi ^a   Smrt, Sean ^a   Honig, Barry ^c   Baek, Kwanghee ^d   Ryu, Sungho ^d   Lorieau, Justin ^a   Kim, You Me ^b,d   Cho, Wonhwa ^a,d  

^a UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

^b Pohang University of Science and Technology (POSTECH)   (South Korea)

^c Columbia University ^*  (United States)

^d Kyung Hee University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING ENERGY; CELL MEMBRANES; ELECTRIC REACTORS; LIPIDS; PROTEINS; SIGNALING; T-CELLS;

ACTIVATION MECHANISMS; ELECTROSTATIC POTENTIAL CALCULATION; HYDROPHOBIC RESIDUES; PHOSPHATIDYLINOSITOL; PHOSPHATIDYLINOSITOL 4 ,5-BISPHOSPHATE; PROTEIN TYROSINE KINASE; SRC HOMOLOGY 2 DOMAINS; SRC HOMOLOGY 3 DOMAINS;

CELL SIGNALING;

MEMBRANE LIPID; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PROTEIN KINASE LCK; T LYMPHOCYTE RECEPTOR; TYROSINE; LYMPHOCYTE ANTIGEN RECEPTOR; PHOSPHATIDYLINOSITOL 3,4,5-TRIPHOSPHATE; POLYPHOSPHOINOSITIDE;

ARTICLE; BINDING AFFINITY; BINDING SITE; CELL MEMBRANE; CONTROLLED STUDY; ELECTRIC POTENTIAL; ENZYME REGULATION; HUMAN; HUMAN CELL; HYDROPHOBICITY; JURKAT CELL LINE; MEMBRANE BINDING; MUTATIONAL ANALYSIS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN INTERACTION; SIGNAL TRANSDUCTION; SRC HOMOLOGY DOMAIN; AMINO ACID SUBSTITUTION; GENETICS; METABOLISM; MISSENSE MUTATION; PHYSIOLOGY;

AMINO ACID SUBSTITUTION; HUMANS; JURKAT CELLS; LYMPHOCYTE SPECIFIC PROTEIN TYROSINE KINASE P56(LCK); MUTATION, MISSENSE; PHOSPHATIDYLINOSITOL 4,5-DIPHOSPHATE; PHOSPHATIDYLINOSITOL PHOSPHATES; RECEPTORS, ANTIGEN, T-CELL; SIGNAL TRANSDUCTION; SRC HOMOLOGY DOMAINS;

EID: 84983436849     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M116.720284     Document Type: Article

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