NMR paper Autophosphorylation of soluble insulin receptor protein-tyrosine kinases. 1H NMR spec

		BioNMR > Educational resources > Journal club
[NMR paper] Autophosphorylation of soluble insulin receptor protein-tyrosine kinases. 1H NMR spec

Webservers

NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

Thread Tools

Search this Thread

Rate Thread

Display Modes

08-21-2010, 11:12 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,714

Points: 193,617, Level: 100

Level up: 0%, 0 Points needed

Activity: 50.7%

Last Achievements

Award-Showcase

NMR Credits: 0

NMR Points: 193,617

Downloads: 0

Uploads: 0

Autophosphorylation of soluble insulin receptor protein-tyrosine kinases. 1H NMR spec

Autophosphorylation of soluble insulin receptor protein-tyrosine kinases. 1H NMR spectral changes observed during phosphorylation of mobile tyrosine residues.

Related Articles Autophosphorylation of soluble insulin receptor protein-tyrosine kinases. 1H NMR spectral changes observed during phosphorylation of mobile tyrosine residues.

J Biol Chem. 1991 Jul 15;266(20):13405-10

Authors: Levine BA, Tavaré JM, Alejos E, Clack B, Sayed N

Autophosphorylation of a soluble approximately 48-kDa derivative of the insulin receptor protein-tyrosine kinase occurs at multiple tyrosine residues (analogous to tyrosines 1158, 1162, and 1163 in the kinase homology region of the native receptor and tyrosines 1328 and 1334 in the carboxyl-terminal tail) and is accompanied by an increase in the specific activity of the enzyme toward exogenous substrates. A comparison of 1H NMR spectra of approximately 48- and approximately 38-kDa forms of enzyme (the latter generated by tryptic deletion of approximately 10 kDa from the carboxyl terminus of the approximately 48-kDa protein) allows a correlation of observed mobile tyrosine resonances to two of the known sites of autophosphorylation (residues 1328 and 1334). Furthermore, spectra acquired during autophosphorylation of the approximately 48-kDa enzyme reveal a rapid downfield shift in the resonances of these mobile tail tyrosines consistent with their phosphorylation (as confirmed by two-dimensional tryptic phosphopeptide mapping performed under identical conditions). This experimental strategy now provides a means by which to monitor protein-tyrosine kinase autophosphorylation in solution in real time.

PMID: 1649190 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] Screening of protein kinases by ATP-STD NMR spectroscopy. Screening of protein kinases by ATP-STD NMR spectroscopy. Related Articles Screening of protein kinases by ATP-STD NMR spectroscopy. J Am Chem Soc. 2005 Jun 8;127(22):7978-9 Authors: McCoy MA, Senior MM, Wyss DF ATP-STD NMR takes advantage of Mg2+ binding to ATP to adjust the ATP affinity for protein kinases permitting a wide range of Ki's to be determined for ATP competitive ligands. Substituting Mn2+ for Mg2+ creates a paramagnetic probe (MnATP) from which the proximity of non-ATP competitive ligands can be inferred. Internal standards and...	nmrlearner	Journal club	0	11-25-2010 08:21 PM
[NMR paper] Novel mechanism of regulation of the non-receptor protein tyrosine kinase Csk: insigh Novel mechanism of regulation of the non-receptor protein tyrosine kinase Csk: insights from NMR mapping studies and site-directed mutagenesis. Related Articles Novel mechanism of regulation of the non-receptor protein tyrosine kinase Csk: insights from NMR mapping studies and site-directed mutagenesis. J Mol Biol. 2001 Nov 16;314(1):129-38 Authors: Shekhtman A, Ghose R, Wang D, Cole PA, Cowburn D Csk (C-terminal Src kinase), a protein tyrosine kinase, consisting of the Src homology 2 and 3 (SH2 and SH3) domains and a catalytic domain,...	nmrlearner	Journal club	0	11-19-2010 08:44 PM
Efficient protein production method for NMR using soluble protein tags with cold shoc Efficient protein production method for NMR using soluble protein tags with cold shock expression vector Abstract The E. coli protein expression system is one of the most useful methods employed for NMR sample preparation. However, the production of some recombinant proteins in E. coli is often hampered by difficulties such as low expression level and low solubility. To address these problems, a modified cold-shock expression system containing a glutathione S-transferase (GST) tag, the pCold-GST system, was investigated. The pCold-GST system successfully expressed 9 out of 10 proteins...	nmrlearner	Journal club	0	09-18-2010 04:53 AM
Efficient protein production method for NMR using soluble protein tags with cold shoc Efficient protein production method for NMR using soluble protein tags with cold shock expression vector. Related Articles Efficient protein production method for NMR using soluble protein tags with cold shock expression vector. J Biomol NMR. 2010 Sep 16; Authors: Hayashi K, Kojima C The E. coli protein expression system is one of the most useful methods employed for NMR sample preparation. However, the production of some recombinant proteins in E. coli is often hampered by difficulties such as low expression level and low solubility. To...	nmrlearner	Journal club	0	09-17-2010 04:14 PM
[NMR paper] Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 ph Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 phosphotyrosine binding domain upon binding to an interleukin 4 receptor phosphopeptide. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 phosphotyrosine binding domain upon binding to an interleukin 4 receptor phosphopeptide. Biochemistry. 1997 Apr 8;36(14):4118-24 Authors: Olejniczak ET, Zhou MM, Fesik SW Proteins recognize...	nmrlearner	Journal club	0	08-22-2010 03:31 PM
[NMR paper] Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 ph Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 phosphotyrosine binding domain upon binding to an interleukin 4 receptor phosphopeptide. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 phosphotyrosine binding domain upon binding to an interleukin 4 receptor phosphopeptide. Biochemistry. 1997 Apr 8;36(14):4118-24 Authors: Olejniczak ET, Zhou MM, Fesik SW Proteins recognize...	nmrlearner	Journal club	0	08-22-2010 03:03 PM
[NMR paper] Comparative 2D NMR studies of human insulin and des-pentapeptide insulin: sequential Comparative 2D NMR studies of human insulin and des-pentapeptide insulin: sequential resonance assignment and implications for protein dynamics and receptor recognition. Related Articles Comparative 2D NMR studies of human insulin and des-pentapeptide insulin: sequential resonance assignment and implications for protein dynamics and receptor recognition. Biochemistry. 1991 Jun 4;30(22):5505-15 Authors: Hua QX, Weiss MA The solution structure and dynamics of human insulin are investigated by 2D 1H NMR spectroscopy in reference to a previously...	nmrlearner	Journal club	0	08-21-2010 11:16 PM
[NMR paper] Autophosphorylation of soluble insulin receptor protein-tyrosine kinases. 1H NMR spec Autophosphorylation of soluble insulin receptor protein-tyrosine kinases. 1H NMR spectral changes observed during phosphorylation of mobile tyrosine residues. Related Articles Autophosphorylation of soluble insulin receptor protein-tyrosine kinases. 1H NMR spectral changes observed during phosphorylation of mobile tyrosine residues. J Biol Chem. 1991 Jul 15;266(20):13405-10 Authors: Levine BA, Tavaré JM, Alejos E, Clack B, Sayed N Autophosphorylation of a soluble approximately 48-kDa derivative of the insulin receptor protein-tyrosine kinase...	nmrlearner	Journal club	0	08-21-2010 11:12 PM

« Previous Thread | Next Thread »

Posting Rules
You may not post new threads You may not post replies You may not post attachments You may not edit your posts BB code is On Smilies are On [IMG] code is On HTML code is On Trackbacks are Off Pingbacks are Off Refbacks are Off