NMR solution structure of the N-terminal domain of hERG and its interaction with the

		BioNMR > Educational resources > Journal club
NMR solution structure of the N-terminal domain of hERG and its interaction with the

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

11-09-2010, 11:29 AM

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

NMR solution structure of the N-terminal domain of hERG and its interaction with the

NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker.

NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker.

Biochem Biophys Res Commun. 2010 Nov 2;

Authors: Li Q, Gayen S, Chen AS, Huang Q, Raida M, Kang C

The human Ether-à-go-go Related Gene (hERG) potassium channel mediates the rapid delayed rectifier current (IKr) in the cardiac action potential. Mutations in the 135 amino acid residue N-terminal domain (NTD) cause channel dysfunction or mis-translocation. To study the structure of NTD, it was overexpressed and purified from E. coli cells using affinity purification and gel filtration chromatography. The purified protein behaved as a monomer under purification conditions. Far- and near-UV, circular dichroism (CD) and solution nuclear magnetic resonance (NMR) studies showed that the purified protein was well-folded. The solution structure of NTD was obtained and the N-terminal residues 13-23 forming an amphipathic helix which may be important for the protein-protein or -membrane interactions. NMR titration experiment also demonstrated that residues from 88 to 94 in NTD are important for the molecular interaction with the peptide derived from the S4-S5 linker.

PMID: 21055387 [PubMed - as supplied by publisher]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
An NMR study of the N-terminal domain of wild-type hERG and a T65P trafficking deficient hERG mutant. An NMR study of the N-terminal domain of wild-type hERG and a T65P trafficking deficient hERG mutant. An NMR study of the N-terminal domain of wild-type hERG and a T65P trafficking deficient hERG mutant. Proteins. 2011 May 16; Authors: Gayen S, Li Q, Chen AS, Nguyen TH, Huang Q, Hill J, Kang C The human Ether-à-go-go Related Gene (hERG) potassium channel plays an important role in the heart by controlling the rapid delayed rectifier current. The N-terminal 135 residues (NTD) contain a Per-Arnt-Sim (PAS) domain and an N-terminal amphipathic helix....	nmrlearner	Journal club	0	06-12-2011 12:15 AM
[NMR paper] NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein. Related Articles NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein. Biochemistry. 2004 Nov 30;43(47):14940-7 Authors: Biverståhl H, Andersson A, Gräslund A, Mäler L The structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein (bPrPp) has been investigated by NMR spectroscopy in phospholipid membrane mimetic systems. CD spectroscopy...	nmrlearner	Journal club	0	11-24-2010 10:03 PM
[NMR paper] Solution NMR structure of the C-terminal domain of the human protein DEK. Solution NMR structure of the C-terminal domain of the human protein DEK. Related Articles Solution NMR structure of the C-terminal domain of the human protein DEK. Protein Sci. 2004 Aug;13(8):2252-9 Authors: Devany M, Kotharu NP, Matsuo H The chromatin-associated protein DEK was first identified as a fusion protein in patients with a subtype of acute myelogenous leukemia. It has since become associated with diverse human ailments ranging from cancers to autoimmune diseases. Despite much research effort, the biochemical basis for these...	nmrlearner	Journal club	0	11-24-2010 09:51 PM
[NMR paper] NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA oligomers. Related Articles NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA oligomers. J Biol Chem. 2004 Jul 23;279(30):31455-61 Authors: Okubo S, Hara F, Tsuchida Y, Shimotakahara S, Suzuki S, Hatanaka H, Yokoyama S, Tanaka H, Yasuda H, Shindo H A member of the PIAS (protein inhibitor of activated STAT) family of proteins, PIAS1, have been reported...	nmrlearner	Journal club	0	11-24-2010 09:51 PM
[NMR paper] Solution structure of the carboxyl-terminal domain of RAP74 and NMR characterization Solution structure of the carboxyl-terminal domain of RAP74 and NMR characterization of the FCP1-binding sites of RAP74 and human TFIIB. Solution structure of the carboxyl-terminal domain of RAP74 and NMR characterization of the FCP1-binding sites of RAP74 and human TFIIB. Biochemistry. 2003 Feb 18;42(6):1460-9 Authors: Nguyen BD, Chen HT, Kobor MS, Greenblatt J, Legault P, Omichinski JG FCP1 (TFIIF-associated CTD phosphatase) is the only known phosphatase specific for the phosphorylated CTD of RNAP II. The phosphatase activity of FCP1 is...	nmrlearner	Journal club	0	11-24-2010 09:01 PM
[NMR paper] Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia col Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR. Biochemistry. 1997 Mar 4;36(9):2517-30 Authors: Garrett DS, Seok YJ, Liao DI, Peterkofsky A, Gronenborn AM, Clore GM ...	nmrlearner	Journal club	0	08-22-2010 03:31 PM
[NMR paper] Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia col Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR. Biochemistry. 1997 Mar 4;36(9):2517-30 Authors: Garrett DS, Seok YJ, Liao DI, Peterkofsky A, Gronenborn AM, Clore GM ...	nmrlearner	Journal club	0	08-22-2010 03:03 PM
[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

« 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