NMR paper 1H NMR evidence that Glu-38 interacts with the N-terminal functional domain in interl

		BioNMR > Educational resources > Journal club
[NMR paper] 1H NMR evidence that Glu-38 interacts with the N-terminal functional domain in interl

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

08-22-2010, 02:20 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

1H NMR evidence that Glu-38 interacts with the N-terminal functional domain in interl

1H NMR evidence that Glu-38 interacts with the N-terminal functional domain in interleukin-8.

Related Articles 1H NMR evidence that Glu-38 interacts with the N-terminal functional domain in interleukin-8.

FEBS Lett. 1996 Dec 9;399(1-2):43-6

Authors: Rajarathnam K, Clark-Lewis I, Dewald B, Baggiolini M, Sykes BD

In order to assess the importance of the buried Glu-38 observed in the structure of interleukin-8, an analog in which Glu-38 was replaced with Ala (E38A analog) was investigated by 1H NMR spectroscopy and neutrophil activation. Detailed analysis of the NMR NOESY data showed that the solution structure of the E38A analog is essentially the same as that for the native protein. Also, the neutrophil elastase activity of the E38A analog was similar to that of the native protein. However, the Gln-8 and Cys-9 amide proton chemical shifts, which are significantly downfield-shifted in the native protein, exhibit more 'normal' values. This observation indicates that in the native protein, Glu-38 side-chain carboxylate interacts with Gln-8 and Cys-9 amide protons. Although the N-terminal residues are critical for function, this interaction is not essential for neutrophil activation.

PMID: 8980116 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
N-terminal Dbl domain of the RhoGEF, Kalirin N-terminal Dbl domain of the RhoGEF, Kalirin N-terminal Dbl domain of the RhoGEF, Kalirin Content Type Journal Article Category NMR structure note Pages 1-8 DOI 10.1007/s10858-012-9605-x Authors	nmrlearner	Journal club	0	02-11-2012 10:31 AM
The Core of Ure2p Prion Fibrils Is Formed by the N-Terminal Segment in a Parallel Cross-? Structure: Evidence from Solid-State NMR. The Core of Ure2p Prion Fibrils Is Formed by the N-Terminal Segment in a Parallel Cross-? Structure: Evidence from Solid-State NMR. The Core of Ure2p Prion Fibrils Is Formed by the N-Terminal Segment in a Parallel Cross-? Structure: Evidence from Solid-State NMR. J Mol Biol. 2011 Apr 8; Authors: Kryndushkin DS, Wickner RB, Tycko R Intracellular fibril formation by Ure2p produces the non-Mendelian genetic element in Saccharomyces cerevisiae, making Ure2p a prion protein. We show that solid-state NMR spectra of full-length Ure2p fibrils, seeded...	nmrlearner	Journal club	0	04-19-2011 11:01 PM
Evidence from solid-state NMR for nonhelical conformations in the transmembrane domain of the amyloid precursor protein. Evidence from solid-state NMR for nonhelical conformations in the transmembrane domain of the amyloid precursor protein. Evidence from solid-state NMR for nonhelical conformations in the transmembrane domain of the amyloid precursor protein. Biophys J. 2011 Feb 2;100(3):711-9 Authors: Lu JX, Yau WM, Tycko R The amyloid precursor protein (APP) is subject to proteolytic processing by ?-secretase within neuronal membranes, leading to Alzheimer's disease-associated ?-amyloid peptide production by cleavage near the midpoint of the*single...	nmrlearner	Journal club	0	02-02-2011 12:40 PM
ESR and NMR studies provide evidence that phosphatidyl glycerol specifically interacts with poxvirus membranes. ESR and NMR studies provide evidence that phosphatidyl glycerol specifically interacts with poxvirus membranes. ESR and NMR studies provide evidence that phosphatidyl glycerol specifically interacts with poxvirus membranes. Virol J. 2010 Dec 31;7(1):379 Authors: Debouzy JC, Crouzier D, Favier AL, Perino J ABSTRACT: BACKGROUND: The lung would be the first organ targeted in case of the use of Variola virus (the causative agent of smallpox) as a bioweapon. Pulmonary surfactant composed of lipids (90%) and proteins (10%) is considered the major...	nmrlearner	Journal club	0	01-05-2011 09:51 PM
[NMR paper] NMR evidence for independent domain structures in zoocin A, an antibacterial exoenzym NMR evidence for independent domain structures in zoocin A, an antibacterial exoenzyme. Related Articles NMR evidence for independent domain structures in zoocin A, an antibacterial exoenzyme. Biochem Biophys Res Commun. 2004 Apr 30;317(2):527-30 Authors: Liang Q, Simmonds RS, Timkovich R NMR was used to obtain spectroscopic evidence supporting a two domain model for zoocin A in which an N-terminal catalytic domain is linked by a threonine-proline rich linker to a target recognition domain responsible for recognizing the cell wall of bacteria...	nmrlearner	Journal club	0	11-24-2010 09:51 PM
[NMR paper] Catalytic activity of the SH2 domain of human pp60c-src; evidence from NMR, mass spec Catalytic activity of the SH2 domain of human pp60c-src; evidence from NMR, mass spectrometry, site-directed mutagenesis and kinetic studies for an inherent phosphatase activity. Related Articles Catalytic activity of the SH2 domain of human pp60c-src; evidence from NMR, mass spectrometry, site-directed mutagenesis and kinetic studies for an inherent phosphatase activity. Biochemistry. 1995 Nov 21;34(46):15351-8 Authors: Boerner RJ, Consler TG, Gampe RT, Weigl D, Willard DH, Davis DG, Edison AM, Loganzo F, Kassel DB, Xu RX During solution...	nmrlearner	Journal club	0	08-22-2010 03:50 AM
[NMR paper] NMR structure and functional studies of the Mu repressor DNA-binding domain. NMR structure and functional studies of the Mu repressor DNA-binding domain. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR structure and functional studies of the Mu repressor DNA-binding domain. Biochemistry. 1999 Jun 29;38(26):8367-76 Authors: Ilangovan U, Wojciak JM, Connolly KM, Clubb RT The repressor protein of bacteriophage Mu establishes and maintains lysogeny by shutting down transposition functions needed for phage DNA replication. It interacts with several repeated DNA...	nmrlearner	Journal club	0	08-21-2010 04:03 PM
[NMR paper] NMR structure of the (52-96) C-terminal domain of the HIV-1 regulatory protein Vpr: m NMR structure of the (52-96) C-terminal domain of the HIV-1 regulatory protein Vpr: molecular insights into its biological functions. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR structure of the (52-96) C-terminal domain of the HIV-1 regulatory protein Vpr: molecular insights into its biological functions. J Mol Biol. 1999 Feb 5;285(5):2105-17 Authors: Schüler W, Wecker K, de Rocquigny H, Baudat Y, Sire J, Roques BP The HIV-1 regulatory protein Vpr (96 amino...	nmrlearner	Journal club	0	08-21-2010 04:03 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