NMR binding and crystal structure reveal that intrinsically-unstructured regulatory domain auto-inhibits PAK4 by a mechanism different from that of PAK1

Biochemical and Biophysical Research Communications

Volumn 438, Issue 1, 2013, Pages 169-174

  Wang, Wei ^a   Lim, Liangzhong ^a   Baskaran, Yohendran ^b   Manser, Ed ^b   Song, Jianxing ^a,c  

^a NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^b INSTITUTE OF MOLECULAR AND CELL BIOLOGY   (Singapore)

^c NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

Author keywords

Auto inhibition; Intrinsically unstructured protein (IUP); Isothermal titration calorimetry (ITC); NMR spectroscopy; P21 activated kinases (PAKs); X ray crystallography

Indexed keywords

P21 ACTIVATED KINASE 1; P21 ACTIVATED KINASE 4;

ALPHA HELIX; ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; HUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL;

AUTO-INHIBITION; INTRINSICALLY UNSTRUCTURED PROTEIN (IUP); ISOTHERMAL TITRATION CALORIMETRY (ITC); NMR SPECTROSCOPY; P21-ACTIVATED KINASES (PAKS); X-RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY; ENZYME INHIBITORS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; P21-ACTIVATED KINASES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN KINASE INHIBITORS;

EID: 84881554400     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.07.047     Document Type: Article

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