Related ArticlesStructure and Backbone Dynamics of vanadate-bound PRL-3: Comparison of 15N NMR Relaxation Profiles of free and vanadate-bound PRL-3.
Biochemistry. 2014 Jul 1;
Authors: Jeong KW, Kang DI, Lee E, Shin A, Jin B, Park YG, Lee CK, Kim EH, Jeon YH, Kim EE, Kim Y
Abstract
Phosphatases of regenerating liver (PRLs) constitute a novel class of small, prenylated phosphatases with oncogenic activity. PRL-3 is particularly important in cancer metastasis and represents a potential, therapeutic target. The flexibility of the WPD loop as well as P-loop of protein tyrosine phosphatases is closely related to their catalytic activity. Using nuclear magnetic resonance (NMR) spectroscopy, we studied the structure of vanadate-bound PRL-3, which was generated by addition of sodium orthovanadate to PRL-3. The WPD loop of free PRL-3 extended outside of the active site, forming an open conformation, whereas that of vanadate-bound PRL-3 was directed into the active site by a large movement, resulting in a closed conformation. We suggest that vanadate binding induced structural changes of the WPD loop, P-loop, ?4-?6 helices, and polybasic region. Compared to free PRL-3, vanadate-bound PRL-3 has a longer ?4 helix, where the catalytic R110 residue coordinates with vanadate in the active site. In addition, the hydrophobic cavity formed by ?4-?6 helices with a depth of 14-15 Å can accommodate a farnesyl chain at the truncated prenylation motif of PRL-3, i.e., from R169 to M173. Conformational exchange data suggested that the WPD loop moves between open and closed conformations with a closing rate constant kclose of 7 s-1. This intrinsic loop flexibility of PRL-3 may be related to their catalytic rate and may play a role in the substrate recognition.
PMID: 24983822 [PubMed - as supplied by publisher]
[NMR paper] Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.
From Mendeley Biomolecular NMR group:
Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.
Biochemistry (1994). Volume: 33, Issue: 19. Pages: 5984-6003. N a Farrow, R Muhandiram, a U Singer, S M Pascal, C M Kay, G Gish, S E Shoelson, T Pawson, J D Forman-Kay, L E Kay et al.
The backbone dynamics of the C-terminal SH2 domain of phospholipase C gamma 1 have been investigated. Two forms of the domain were studied, one in complex with a high-affinity binding peptide derived from the platelet-derived growth factor receptor and the...
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[NMR paper] Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.
From Mendeley Biomolecular NMR group:
Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.
Biochemistry (1994). Volume: 33, Issue: 19. Pages: 5984-6003. N a Farrow, R Muhandiram, a U Singer, S M Pascal, C M Kay, G Gish, S E Shoelson, T Pawson, J D Forman-Kay, L E Kay et al.
The backbone dynamics of the C-terminal SH2 domain of phospholipase C gamma 1 have been investigated. Two forms of the domain were studied, one in complex with a high-affinity binding peptide derived from the platelet-derived growth factor receptor and the...
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11-22-2012 11:49 AM
[NMR paper] NMR structure of alpha-bungarotoxin free and bound to a mimotope of the nicotinic ace
NMR structure of alpha-bungarotoxin free and bound to a mimotope of the nicotinic acetylcholine receptor.
Related Articles NMR structure of alpha-bungarotoxin free and bound to a mimotope of the nicotinic acetylcholine receptor.
Biochemistry. 2002 Feb 5;41(5):1457-63
Authors: Scarselli M, Spiga O, Ciutti A, Bernini A, Bracci L, Lelli B, Lozzi L, Calamandrei D, Di Maro D, Klein S, Niccolai N
A combinatorial library approach was used to produce synthetic peptides mimicking the snake neurotoxin binding site of nicotinic receptors. Among the...
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11-24-2010 08:49 PM
[NMR paper] 15N NMR relaxation studies of free and ligand-bound human acidic fibroblast growth fa
15N NMR relaxation studies of free and ligand-bound human acidic fibroblast growth factor.
Related Articles 15N NMR relaxation studies of free and ligand-bound human acidic fibroblast growth factor.
J Biol Chem. 2000 Dec 15;275(50):39444-50
Authors: Chi Y, Kumar TK, Chiu IM, Yu C
15N NMR relaxation data have been used to characterize the backbone dynamics of the human acidic fibroblast growth factor (hFGF-1) in its free and sucrose octasulfate (SOS)-bound states. (15)N longitudinal (R(1)), transverse (R(2)) relaxation rates and (1H)-(15)N...
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11-19-2010 08:29 PM
[NMR paper] NMR structure of human erythropoietin and a comparison with its receptor bound confor
NMR structure of human erythropoietin and a comparison with its receptor bound conformation.
Related Articles NMR structure of human erythropoietin and a comparison with its receptor bound conformation.
Nat Struct Biol. 1998 Oct;5(10):861-6
Authors: Cheetham JC, Smith DM, Aoki KH, Stevenson JL, Hoeffel TJ, Syed RS, Egrie J, Harvey TS
The solution structure of human erythropoietin (EPO) has been determined by nuclear magnetic resonance spectroscopy and the overall topology of the protein is revealed as a novel combination of features taken from...
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11-17-2010 11:15 PM
[NMR paper] 15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase:
15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase: backbone dynamics and entropy changes of an enzyme upon inhibitor binding.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles 15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase: backbone dynamics and entropy changes of an enzyme upon inhibitor binding.
Biochemistry. 1996 Dec 17;35(50):16036-47
Authors: Stivers JT, Abeygunawardana C, Mildvan AS
The solution secondary...
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[NMR paper] 51V NMR study of vanadate binding to myosin and its subfragment 1.
51V NMR study of vanadate binding to myosin and its subfragment 1.
Related Articles 51V NMR study of vanadate binding to myosin and its subfragment 1.
Biochemistry. 1990 Sep 25;29(38):9091-6
Authors: Ringel I, Peyser YM, Muhlrad A
The binding of various forms of vanadate to myosin and myosin subfragment 1 (S-1) was studied by 51V NMR at increasing vanadate concentrations between 0.06 and 1.0 mM. The distribution of the various forms of vanadate in the solution depended on the total concentration of vanadate. At low concentrations, the...