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

10.1016/j.bbrc.2013.07.047

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Main Authors:	Wang, W., Lim, L., Baskaran, Y., Manser, E., Song, J.
Other Authors:	BIOLOGICAL SCIENCES
Format:	Article
Published:	2014
Subjects:	Auto-inhibition Intrinsically unstructured protein (IUP) Isothermal titration calorimetry (ITC) NMR spectroscopy P21-activated kinases (PAKs) X-ray crystallography
Online Access:	http://scholarbank.nus.edu.sg/handle/10635/101228
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Institution:	National University of Singapore

id	sg-nus-scholar.10635-101228
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spelling	sg-nus-scholar.10635-1012282023-10-26T08:27:03Z NMR binding and crystal structure reveal that intrinsically-unstructured regulatory domain auto-inhibits PAK4 by a mechanism different from that of PAK1 Wang, W. Lim, L. Baskaran, Y. Manser, E. Song, J. BIOLOGICAL SCIENCES Auto-inhibition Intrinsically unstructured protein (IUP) Isothermal titration calorimetry (ITC) NMR spectroscopy P21-activated kinases (PAKs) X-ray crystallography 10.1016/j.bbrc.2013.07.047 Biochemical and Biophysical Research Communications 438 1 169-174 BBRCA 2014-10-27T08:34:55Z 2014-10-27T08:34:55Z 2013-08-16 Article Wang, W., Lim, L., Baskaran, Y., Manser, E., Song, J. (2013-08-16). 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 438 (1) : 169-174. ScholarBank@NUS Repository. https://doi.org/10.1016/j.bbrc.2013.07.047 0006291X http://scholarbank.nus.edu.sg/handle/10635/101228 000323467100029 Scopus
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	Auto-inhibition Intrinsically unstructured protein (IUP) Isothermal titration calorimetry (ITC) NMR spectroscopy P21-activated kinases (PAKs) X-ray crystallography
spellingShingle	Auto-inhibition Intrinsically unstructured protein (IUP) Isothermal titration calorimetry (ITC) NMR spectroscopy P21-activated kinases (PAKs) X-ray crystallography Wang, W. Lim, L. Baskaran, Y. Manser, E. Song, J. NMR binding and crystal structure reveal that intrinsically-unstructured regulatory domain auto-inhibits PAK4 by a mechanism different from that of PAK1
description	10.1016/j.bbrc.2013.07.047
author2	BIOLOGICAL SCIENCES
author_facet	BIOLOGICAL SCIENCES Wang, W. Lim, L. Baskaran, Y. Manser, E. Song, J.
format	Article
author	Wang, W. Lim, L. Baskaran, Y. Manser, E. Song, J.
author_sort	Wang, W.
title	NMR binding and crystal structure reveal that intrinsically-unstructured regulatory domain auto-inhibits PAK4 by a mechanism different from that of PAK1
title_short	NMR binding and crystal structure reveal that intrinsically-unstructured regulatory domain auto-inhibits PAK4 by a mechanism different from that of PAK1
title_full	NMR binding and crystal structure reveal that intrinsically-unstructured regulatory domain auto-inhibits PAK4 by a mechanism different from that of PAK1
title_fullStr	NMR binding and crystal structure reveal that intrinsically-unstructured regulatory domain auto-inhibits PAK4 by a mechanism different from that of PAK1
title_full_unstemmed	NMR binding and crystal structure reveal that intrinsically-unstructured regulatory domain auto-inhibits PAK4 by a mechanism different from that of PAK1
title_sort	nmr binding and crystal structure reveal that intrinsically-unstructured regulatory domain auto-inhibits pak4 by a mechanism different from that of pak1
publishDate	2014
url	http://scholarbank.nus.edu.sg/handle/10635/101228
_version_	1781787349305262080

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

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