NMR paper NMR solution structure of the isolated Apo Pin1 WW domain: comparison to the x-ray cr

		BioNMR > Educational resources > Journal club
[NMR paper] NMR solution structure of the isolated Apo Pin1 WW domain: comparison to the x-ray cr

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

11-24-2010, 08:49 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

NMR solution structure of the isolated Apo Pin1 WW domain: comparison to the x-ray cr

NMR solution structure of the isolated Apo Pin1 WW domain: comparison to the x-ray crystal structures of Pin1.

Related Articles NMR solution structure of the isolated Apo Pin1 WW domain: comparison to the x-ray crystal structures of Pin1.

Biopolymers. 2002 Feb;63(2):111-21

Authors: Kowalski JA, Liu K, Kelly JW

The NMR solution structure of the isolated Apo Pin1 WW domain (6-39) reveals that it adopts a twisted three-stranded antiparallel beta-sheet conformation, very similar to the structure exhibited by the crystal of this domain in the context of the two domain Pin1 protein. While the B factors in the apo x-ray crystal structure indicate that loop 1 and loop 2 are conformationally well defined, the solution NMR data suggest that loop 1 is quite flexible, at least in the absence of the ligand. The NMR chemical shift and nuclear Overhauser effect pattern exhibited by the 6-39 Pin1 WW domain has proven to be diagnostic for demonstrating that single site variants of this domain adopt a normally folded structure. Knowledge of this type is critical before embarking on time-consuming kinetic and thermodynamic studies required for a detailed understanding of beta-sheet folding.

PMID: 11786999 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis. Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis. Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis. J Biomol NMR. 2011 Sep;51(1-2):21-34 Authors: Greenwood AI, Rogals MJ, De S, Lu KP, Kovrigin EL, Nicholson LK Abstract The phosphorylation-specific peptidyl-prolyl isomerase Pin1 catalyzes the isomerization of the peptide bond preceding a proline residue between cis and trans isomers. To best understand the mechanisms of Pin1 regulation,...	nmrlearner	Journal club	0	09-30-2011 06:00 AM
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis. Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis. Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis. J Biomol NMR. 2011 Sep;51(1-2):21-34 Authors: Greenwood AI, Rogals MJ, De S, Lu KP, Kovrigin EL, Nicholson LK Abstract The phosphorylation-specific peptidyl-prolyl isomerase Pin1 catalyzes the isomerization of the peptide bond preceding a proline residue between cis and trans isomers. To best understand the mechanisms of Pin1 regulation,...	nmrlearner	Journal club	0	09-30-2011 05:59 AM
[NMR paper] Interpretation of NMR relaxation properties of Pin1, a two-domain protein, based on B Interpretation of NMR relaxation properties of Pin1, a two-domain protein, based on Brownian dynamic simulations. Related Articles Interpretation of NMR relaxation properties of Pin1, a two-domain protein, based on Brownian dynamic simulations. J Biomol NMR. 2004 May;29(1):21-35 Authors: Bernadó P, Fernandes MX, Jacobs DM, Fiebig K, García de la Torre J, Pons M Many important proteins contain multiple domains connected by flexible linkers. Inter-domain motion is suggested to play a key role in many processes involving molecular recognition....	nmrlearner	Journal club	0	11-24-2010 09:51 PM
[NMR paper] 1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides. 1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides. Related Articles 1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides. J Biol Chem. 2001 Jul 6;276(27):25150-6 Authors: Wintjens R, Wieruszeski JM, Drobecq H, Rousselot-Pailley P, Buée L, Lippens G, Landrieu I The recent crystal structure of Pin1 protein bound to a doubly phosphorylated peptide from the C-terminal domain of RNA polymerase II revealed that binding interactions between Pin1 and its substrate take place through its...	nmrlearner	Journal club	0	11-19-2010 08:32 PM
[NMR paper] NMR structure of a stable "OB-fold" sub-domain isolated from staphylococcal nuclease. NMR structure of a stable "OB-fold" sub-domain isolated from staphylococcal nuclease. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR structure of a stable "OB-fold" sub-domain isolated from staphylococcal nuclease. J Mol Biol. 1995 Jul 7;250(2):134-43 Authors: Alexandrescu AT, Gittis AG, Abeygunawardana C, Shortle D Similar folds often occur in proteins with dissimilar sequences. The OB-fold forms a part of the structures of at least seven non-homologous proteins...	nmrlearner	Journal club	0	08-22-2010 03:50 AM
[NMR paper] NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Ev NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Evidence of trifluoroethanol induced native-like beta-hairpin formation. Related Articles NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Evidence of trifluoroethanol induced native-like beta-hairpin formation. Biochemistry. 1994 May 17;33(19):6004-14 Authors: Blanco FJ, JimÃ©nez MA, Pineda A, Rico M, Santoro J, Nieto JL The solution structure of the isolated N-terminal fragment of streptococcal protein-G B1 domain has been...	nmrlearner	Journal club	0	08-22-2010 03:33 AM
[NMR paper] NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Ev NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Evidence of trifluoroethanol induced native-like beta-hairpin formation. Related Articles NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Evidence of trifluoroethanol induced native-like beta-hairpin formation. Biochemistry. 1994 May 17;33(19):6004-14 Authors: Blanco FJ, JimÃ©nez MA, Pineda A, Rico M, Santoro J, Nieto JL The solution structure of the isolated N-terminal fragment of streptococcal protein-G B1 domain has been...	nmrlearner	Journal club	0	08-22-2010 03:33 AM
[NMR paper] The NMR structure of the activation domain isolated from porcine procarboxypeptidase The NMR structure of the activation domain isolated from porcine procarboxypeptidase B. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles The NMR structure of the activation domain isolated from porcine procarboxypeptidase B. EMBO J. 1991 Jan;10(1):11-5 Authors: Vendrell J, Billeter M, Wider G, AvilÃ©s FX, WÃ¼thrich K The three-dimensional structure of the activation domain isolated from porcine pancreatic procarboxypeptidase B was determined using 1H NMR...	nmrlearner	Journal club	0	08-21-2010 11:16 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