NMR paper [1H,13C] NMR determination of the order of lobe loading of human transferrin with iro

		BioNMR > Educational resources > Journal club
[NMR paper] [1H,13C] NMR determination of the order of lobe loading of human transferrin with iro

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

11-17-2010, 11:06 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,777

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,13C] NMR determination of the order of lobe loading of human transferrin with iro

[1H,13C] NMR determination of the order of lobe loading of human transferrin with iron: comparison with other metal ions.

Related Articles [1H,13C] NMR determination of the order of lobe loading of human transferrin with iron: comparison with other metal ions.

FEBS Lett. 1998 Feb 6;422(3):315-20

Authors: Sun H, Cox MC, Li H, Mason AB, Woodworth RC, Sadler PJ

Human serum transferrin (hTF) is a single-chain bilobal glycoprotein (80 kDa) which transports Fe3+ and a variety of other metal ions in blood. Only diferric transferrin, not the apo-protein, binds strongly to transferrin receptors and is taken up by cells via receptor-mediated endocytosis. We show here that 2D [1H,13C] NMR studies of recombinant epsilon-[13C]Met-hTF allow the order of lobe loading with various metal ions, including Fe3+, to be determined. In particular, the resonance for Met-464, a residue in the hydrophobic patch of helix 5, is very sensitive to iron binding in the C-lobe. The selectivity of lobe loading with Fe3+ is compared to loading with Fe2+ (which binds as Fe3+), Al3+, Ga3+ and Bi3+. Similar changes in shifts of the Met residues are observed for these metal ions, suggesting that they induce similar conformational changes in the protein.

PMID: 9498807 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] Determination of protein structures consistent with NMR order parameters. Determination of protein structures consistent with NMR order parameters. Related Articles Determination of protein structures consistent with NMR order parameters. J Am Chem Soc. 2004 Jul 7;126(26):8090-1 Authors: Best RB, Vendruscolo M Order parameters obtained from NMR experiments characterize distributions of bond vector orientations. Their interpretation, however, usually requires the assumption of a particular motional model. We propose a multiple-copy simulation method in which the experimental order parameters are used as restraints in...	nmrlearner	Journal club	0	11-24-2010 09:51 PM
[NMR paper] [13C]Methionine NMR and metal-binding studies of recombinant human transferrin N-lobe Methionine NMR and metal-binding studies of recombinant human transferrin N-lobe and five methionine mutants: conformational changes and increased sensitivity to chloride. Related Articles Methionine NMR and metal-binding studies of recombinant human transferrin N-lobe and five methionine mutants: conformational changes and increased sensitivity to chloride. Biochem J. 1999 Dec 15;344 Pt 3:881-7 Authors: He QY, Mason AB, Tam BM, MacGillivray RT, Woodworth RC The N-lobe of human serum transferrin (hTF/2N) and single point mutants in which each...	nmrlearner	Journal club	0	11-18-2010 08:31 PM
[NMR paper] Identification of platination sites on human serum transferrin using (13)C and (15)N Identification of platination sites on human serum transferrin using (13)C and (15)N NMR spectroscopy. Related Articles Identification of platination sites on human serum transferrin using (13)C and (15)N NMR spectroscopy. J Biol Inorg Chem. 1999 Oct;4(5):621-31 Authors: Cox MC, Barnham KJ, Frenkiel TA, Hoeschele JD, Mason AB, He QY, Woodworth RC, Sadler PJ Reactions between various apo and metal-bound forms of human serum transferrin (80 kDa) and the recombinant N-lobe (40 kDa) with or cis- have been investigated in solution via observation...	nmrlearner	Journal club	0	11-18-2010 08:31 PM
[NMR paper] Defining long range order in NMR structure determination from the dependence of heter Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy. Related Articles Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy. Nat Struct Biol. 1997 Jun;4(6):443-9 Authors: Tjandra N, Garrett DS, Gronenborn AM, Bax A, Clore GM Structure determination by NMR presently relies on short range restraints between atoms in close spatial proximity, principally in the...	nmrlearner	Journal club	0	08-22-2010 03:31 PM
[NMR paper] Trp128Tyr mutation in the N-lobe of recombinant human serum transferrin: 1H- and 15N- Trp128Tyr mutation in the N-lobe of recombinant human serum transferrin: 1H- and 15N-NMR and metal binding studies. Related Articles Trp128Tyr mutation in the N-lobe of recombinant human serum transferrin: 1H- and 15N-NMR and metal binding studies. Protein Eng. 1997 May;10(5):583-91 Authors: Beatty EJ, Cox MC, Frenkiel TA, He QY, Mason AB, Sadler PJ, Tucker A, Woodworth RC The conserved Trp residue within helix 5 of the N-lobe of human serum transferrin (hTF/2N, 40 kDa) has been mutated to Tyr. NMR and CD spectra and energy calculations show...	nmrlearner	Journal club	0	08-22-2010 03:31 PM
[NMR paper] Defining long range order in NMR structure determination from the dependence of heter Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy. Related Articles Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy. Nat Struct Biol. 1997 Jun;4(6):443-9 Authors: Tjandra N, Garrett DS, Gronenborn AM, Bax A, Clore GM Structure determination by NMR presently relies on short range restraints between atoms in close spatial proximity, principally in the...	nmrlearner	Journal club	0	08-22-2010 03:03 PM
[NMR paper] Trp128Tyr mutation in the N-lobe of recombinant human serum transferrin: 1H- and 15N- Trp128Tyr mutation in the N-lobe of recombinant human serum transferrin: 1H- and 15N-NMR and metal binding studies. Related Articles Trp128Tyr mutation in the N-lobe of recombinant human serum transferrin: 1H- and 15N-NMR and metal binding studies. Protein Eng. 1997 May;10(5):583-91 Authors: Beatty EJ, Cox MC, Frenkiel TA, He QY, Mason AB, Sadler PJ, Tucker A, Woodworth RC The conserved Trp residue within helix 5 of the N-lobe of human serum transferrin (hTF/2N, 40 kDa) has been mutated to Tyr. NMR and CD spectra and energy calculations show...	nmrlearner	Journal club	0	08-22-2010 03:03 PM
[NMR paper] Oxalate- and Ga(3+)-induced structural changes in human serum transferrin and its rec Oxalate- and Ga(3+)-induced structural changes in human serum transferrin and its recombinant N-lobe. 1H NMR detection of preferential C-lobe Ga3+ binding. Related Articles Oxalate- and Ga(3+)-induced structural changes in human serum transferrin and its recombinant N-lobe. 1H NMR detection of preferential C-lobe Ga3+ binding. Biochemistry. 1993 Apr 6;32(13):3387-95 Authors: Kubal G, Mason AB, Patel SU, Sadler PJ, Woodworth RC (1) The binding of the synergistic anion oxalate and Ga3+ to human serum transferrin (HTF, 80 kDa) and its recombinant...	nmrlearner	Journal club	0	08-21-2010 11:53 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