NMR paper Evidence for novel action at the cell binding site of human Angiogenin revealed by heteronuclear NMR spectroscopy, in silico and in vivo studies.

		BioNMR > Educational resources > Journal club
[NMR paper] Evidence for novel action at the cell binding site of human Angiogenin revealed by heteronuclear NMR spectroscopy, in silico and in vivo studies.

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

01-10-2018, 12:45 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,732

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

Evidence for novel action at the cell binding site of human Angiogenin revealed by heteronuclear NMR spectroscopy, in silico and in vivo studies.

Evidence for novel action at the cell binding site of human Angiogenin revealed by heteronuclear NMR spectroscopy, in silico and in vivo studies.

Evidence for novel action at the cell binding site of human Angiogenin revealed by heteronuclear NMR spectroscopy, in silico and in vivo studies.

ChemMedChem. 2018 Jan 04;:

Authors: Chatzileontiadou DS, Tsika AC, Diamantopoulou Z, Delbé J, Badet J, Courty J, Skamnaki VT, Parmenopoulou V, Komiotis D, Hayes JM, Spyroulias GA, Leonidas DD

Abstract
A member of Ribonuclease A superfamily, human Angiogenin (hAng) is a potent angiogenic factor. Heteronuclear NMR spectroscopy combined with induced-fit docking revealed a dual binding mode for the most antiangiogenic compound of a series of ribofuranosyl pyrimidine nucleosides that strongly inhibit hAng's angiogenic activity in vivo. While modelling suggests the potential of a simultaneous binding of the inhibitors at the active and cell binding sites, NMR indicates greater affinity for the cell binding site than for the active site. Additionally, a 100 nanoseconds molecular dynamics simulation have confirmed the stability of the binding at the cell-binding site with the predicted protein-ligand interactions in excellent agreement with the NMR data. This is the first time that a nucleoside inhibitor is reported to inhibit completely the angiogenic activity of hAng in vivo by exerting dual inhibitory activity on hAng, blocking both the entrance of hAng into the cell and the ribonucleolytic activity.

PMID: 29314771 [PubMed - as supplied by publisher]

More...

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] Structural Determinants in the Binding of BB2 Receptor Ligands: In Silico, X-Ray and NMR Studies in PD176252 Analogues. Structural Determinants in the Binding of BB2 Receptor Ligands: In Silico, X-Ray and NMR Studies in PD176252 Analogues. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.eurekaselect.com-sites-all-themes-eurekaselect-images-ben_pubmed_flag1.gif Related Articles Structural Determinants in the Binding of BB2 Receptor Ligands: In Silico, X-Ray and NMR Studies in PD176252 Analogues. Curr Top Med Chem. 2017;17(14):1599-1610 Authors: Carrieri A, Lacivita E, Belviso BD, Caliandro R, Mastrorilli P, Gallo V, Niso M, Leopoldo M ...	nmrlearner	Journal club	0	07-06-2017 04:24 PM
[NMR paper] NMR study of Met-1 human Angiogenin: (1)H, (13)C, (15)N backbone and side-chain resonance assignment. NMR study of Met-1 human Angiogenin: (1)H, (13)C, (15)N backbone and side-chain resonance assignment. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR study of Met-1 human Angiogenin: (1)H, (13)C, (15)N backbone and side-chain resonance assignment. Biomol NMR Assign. 2016 Sep 13; Authors: Tsika AC, Chatzileontiadou DS, Leonidas DD, Spyroulias GA Abstract Here, we report the high yield expression and preliminary structural...	nmrlearner	Journal club	0	09-22-2016 06:31 AM
[NMR paper] Mapping Functional Interaction Sites of Human Prune C-Terminal Domain by NMR Spectroscopy in Human Cell Lysates. Mapping Functional Interaction Sites of Human Prune C-Terminal Domain by NMR Spectroscopy in Human Cell Lysates. Mapping Functional Interaction Sites of Human Prune C-Terminal Domain by NMR Spectroscopy in Human Cell Lysates. Chemistry. 2013 Aug 12; Authors: Diana D, Smaldone G, De Antonellis P, Pirone L, Carotenuto M, Alonzi A, Di Gaetano S, Zollo M, Pedone EM, Fattorusso R Abstract Get well prune: The C-terminal third domain of h-prune is largely unfolded and involved in relevant protein-protein interactions, particularly with...	nmrlearner	Journal club	0	08-14-2013 05:24 PM
NMR Studies of the Interactionbetween Human Programmed Cell Death 5 and Human p53 NMR Studies of the Interactionbetween Human Programmed Cell Death 5 and Human p53 http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi201822x/aop/images/medium/bi-2011-01822x_0006.gif Biochemistry DOI: 10.1021/bi201822x http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/EP2xmvNmj2Q More...	nmrlearner	Journal club	0	03-20-2012 10:52 PM
[NMR paper] Over-expression and purification of isotopically labeled recombinant ligand-binding domain of orphan nuclear receptor human B1-binding factor/human liver receptor homologue 1 for NMR studies. Over-expression and purification of isotopically labeled recombinant ligand-binding domain of orphan nuclear receptor human B1-binding factor/human liver receptor homologue 1 for NMR studies. Related Articles Over-expression and purification of isotopically labeled recombinant ligand-binding domain of orphan nuclear receptor human B1-binding factor/human liver receptor homologue 1 for NMR studies. Protein Expr Purif. 2006 Jan;45(1):99-106 Authors: Chen X, Tong X, Xie Y, Wang Y, Ma J, Gao D, Wu H, Chen H The human hepatitis B virus enhancer II...	nmrlearner	Journal club	0	12-01-2010 06:56 PM
[NMR paper] (19)F NMR studies of the leucine-isoleucine-valine binding protein: evidence that a c (19)F NMR studies of the leucine-isoleucine-valine binding protein: evidence that a closed conformation exists in solution. Related Articles (19)F NMR studies of the leucine-isoleucine-valine binding protein: evidence that a closed conformation exists in solution. J Biomol Struct Dyn. 2003 Oct;21(2):235-46 Authors: Salopek-Sondi B, Vaughan MD, Skeels MC, Honek JF, Luck LA The leucine-isoleucine-valine binding protein (LIV) found in the periplasmic space of E. coli has been used as a structural model for a number of neuronal receptors. This...	nmrlearner	Journal club	0	11-24-2010 09:16 PM
[NMR paper] Heteronuclear NMR studies of E. coli translation initiation factor IF3. Evidence that Heteronuclear NMR studies of E. coli translation initiation factor IF3. Evidence that the inter-domain region is disordered in solution. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Heteronuclear NMR studies of E. coli translation initiation factor IF3. Evidence that the inter-domain region is disordered in solution. J Mol Biol. 1997 Feb 14;266(1):15-22 Authors: Moreau M, de Cock E, Fortier PL, Garcia C, Albaret C, Blanquet S, Lallemand JY, Dardel F Initiation...	nmrlearner	Journal club	0	08-22-2010 03:31 PM
[NMR paper] Heteronuclear NMR studies of E. coli translation initiation factor IF3. Evidence that Heteronuclear NMR studies of E. coli translation initiation factor IF3. Evidence that the inter-domain region is disordered in solution. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Heteronuclear NMR studies of E. coli translation initiation factor IF3. Evidence that the inter-domain region is disordered in solution. J Mol Biol. 1997 Feb 14;266(1):15-22 Authors: Moreau M, de Cock E, Fortier PL, Garcia C, Albaret C, Blanquet S, Lallemand JY, Dardel F Initiation...	nmrlearner	Journal club	0	08-22-2010 03:03 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