The intrinsically disordered structural platform of the plant defence hub protein RPM1-interacting protein 4 provides insights into its mode of action in the host-pathogen interface and evolution of the nitrate-induced domain protein family

FEBS Journal

Volumn 281, Issue 17, 2014, Pages 3955-3979

  Sun, Xiaolin ^a   Greenwood, David R ^b,c   Templeton, Matthew D ^b,c   Libich, David S ^d,i   McGhie, Tony K ^a   Xue, Bin ^e   Yoon, Minsoo ^b   Cui, Wei ^b   Kirk, Christopher A ^a   Jones, William T ^a   Uversky, Vladimir N ^f,g,h   Rikkerink, Erik H A ^b  

^a THE NEW ZEALAND INSTITUTE FOR PLANT AND FOOD RESEARCH LIMITED   (New Zealand)

^b PFR   (New Zealand)

^c UNIVERSITY OF AUCKLAND   (New Zealand)

^d MASSEY UNIVERSITY   (New Zealand)

^e UNIVERSITY OF SOUTH FLORIDA   (United States)

^f UNIVERSITY OF SOUTH FLORIDA   (United States)

^g INSTITUTE FOR BIOLOGICAL INSTRUMENTATION   (Russian Federation)

^h KING ABDULAZIZ UNIVERSITY   (Saudi Arabia)

ⁱ NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

binding induced folding; intrinsic disorder; molecular recognition features (MoRFs); plant microbe interaction; RIN4

Indexed keywords

BINDING-INDUCED FOLDING; INTRINSIC DISORDER; MOLECULAR RECOGNITION FEATURES (MORFS); PLANT-MICROBE INTERACTION; RIN4;

AMINO ACID SEQUENCE; ARABIDOPSIS PROTEINS; CARRIER PROTEINS; CIRCULAR DICHROISM; HOST-PATHOGEN INTERACTIONS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; INTRINSICALLY DISORDERED PROTEINS; PLANT PROTEINS; PLANTS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; TEMPERATURE; TRIFLUOROETHANOL; TRYPSIN;

EID: 84906861024     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12937     Document Type: Article

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