BioNMR
NMR aggregator & online community since 2003
BioNMR    
Learn or help to learn NMR - get free NMR books!
 

Go Back   BioNMR > Educational resources > Journal club
Advanced Search



Jobs Groups Conferences Literature Pulse sequences Software forums Programs Sample preps Web resources BioNMR issues


Webservers
NMR processing:
MDD
NMR assignment:
Backbone:
Autoassign
MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
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:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
PROSESS
CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
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:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


Reply
Thread Tools Search this Thread Rate Thread Display Modes
  #1  
Unread 11-24-2010, 08:49 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,137
Points: 193,617, Level: 100
Points: 193,617, Level: 100 Points: 193,617, Level: 100 Points: 193,617, Level: 100
Level up: 0%, 0 Points needed
Level up: 0% Level up: 0% Level up: 0%
Activity: 50.7%
Activity: 50.7% Activity: 50.7% Activity: 50.7%
Last Achievements
Award-Showcase
NMR Credits: 0
NMR Points: 193,617
Downloads: 0
Uploads: 0
Default 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
Reply With Quote


Did you find this post helpful? Yes | No

Reply
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, Jiménez 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, Jiménez 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, Avilés FX, Wüthrich 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


Thread Tools Search this Thread
Search this Thread:

Advanced Search
Display Modes Rate This Thread
Rate This 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



BioNMR advertisements to pay for website hosting and domain registration. Nobody does it for us.



Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Copyright, BioNMR.com, 2003-2013
Search Engine Friendly URLs by vBSEO 3.6.0

All times are GMT. The time now is 10:44 AM.


Map