Solution NMR structure and dynamics of human apo-S100A1 protein.

		BioNMR > Educational resources > Journal club
Solution NMR structure and dynamics of human apo-S100A1 protein.

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

02-08-2011, 06:28 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

Solution NMR structure and dynamics of human apo-S100A1 protein.

Solution NMR structure and dynamics of human apo-S100A1 protein.

Solution NMR structure and dynamics of human apo-S100A1 protein.

J Struct Biol. 2011 Feb 2;

Authors: Nowakowski M, Jaremko L, Jaremko M, Zhukov I, Belczyk A, Bierzy?ski A, Ejchart A

S100A1 belongs to the EF-hand superfamily of calcium binding proteins. It is a representative of the S100 protein family based on amino acid sequence, three-dimensional structure, and biological function as a calcium signal transmitter. It is a homodimer of noncovalently bound subunits. S100A1, like most of other members of the S100 protein family, is a multifunctional, regulatory protein involved in a large variety of biological processes and closely associated with several human diseases. The three-dimensional structure of human apo-(i.e. calcium free)-S100A1 protein was determined by NMR spectroscopy (PDB 2L0P) and its backbone dynamics established by (15)N magnetic relaxation. Comparison of these results with the structure and backbone dynamics previously determined for bovine apo-S100A1 protein modified by disulfide formation with ?-mercaptoethanol at Cys85 revealed that the secondary structure of both these proteins was almost identical, whereas the global structure of the latter was much more mobile than that of human apo-S100 protein. Differences between the structures of human and rat apo-S100A1 are also discussed.

PMID: 21296671 [PubMed - as supplied by publisher]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Solution structure of the human Tax-interacting protein-1 Solution structure of the human Tax-interacting protein-1 Solution structure of the human Tax-interacting protein-1 Content Type Journal Article Pages 329-334 DOI 10.1007/s10858-009-9361-8 Authors	nmrlearner	Journal club	0	01-09-2011 12:46 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] Three-dimensional solution structure of the calcium-signaling protein apo-S100A1 as d Three-dimensional solution structure of the calcium-signaling protein apo-S100A1 as determined by NMR. Related Articles Three-dimensional solution structure of the calcium-signaling protein apo-S100A1 as determined by NMR. Biochemistry. 2002 Jan 22;41(3):788-96 Authors: Rustandi RR, Baldisseri DM, Inman KG, Nizner P, Hamilton SM, Landar A, Landar A, Zimmer DB, Weber DJ S100A1, a member of the S100 protein family, is an EF-hand containing Ca(2+)-binding protein (93 residues per subunit) with noncovalent interactions at its dimer interface. Each...	nmrlearner	Journal club	0	11-24-2010 08:49 PM
[NMR paper] Characterization of the structure and dynamics of amyloidogenic variants of human lys Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy. Related Articles Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy. Protein Sci. 2001 Dec;10(12):2525-30 Authors: Chamberlain AK, Receveur V, Spencer A, Redfield C, Dobson CM The structures and dynamics of the native states of two mutational variants of human lysozyme, I56T and D67H, both associated with non-neuropathic systemic amyloidosis, have been investigated by NMR...	nmrlearner	Journal club	0	11-19-2010 08:44 PM
[NMR paper] NMR solution structure of type II human cellular retinoic acid binding protein: impli NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding. Related Articles NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding. Biochemistry. 1998 Sep 15;37(37):12727-36 Authors: Wang L, Li Y, Abildgaard F, Markley JL, Yan H The structure of human apo-cellular retinoic acid binding protein II (apo-CRABPII) in solution at pH 7.3 has been determined by NMR spectroscopy. The sequential assignments of the 1H, 13C, and 15N resonances...	nmrlearner	Journal club	0	11-17-2010 11:15 PM
[NMR paper] Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) f Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) from Escherichia coli: evidence for conformational dynamics in the single-stranded RNA-binding site. Related Articles Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) from Escherichia coli: evidence for conformational dynamics in the single-stranded RNA-binding site. Biochemistry. 1998 Aug 4;37(31):10881-96 Authors: Feng W, Tejero R, Zimmerman DE, Inouye M, Montelione GT The major cold-shock protein (CspA) from Escherichia...	nmrlearner	Journal club	0	11-17-2010 11:15 PM
[NMR paper] Structure and dynamics of the human granulocyte colony-stimulating factor determined Structure and dynamics of the human granulocyte colony-stimulating factor determined by NMR spectroscopy. Loop mobility in a four-helix-bundle protein. Related Articles Structure and dynamics of the human granulocyte colony-stimulating factor determined by NMR spectroscopy. Loop mobility in a four-helix-bundle protein. Biochemistry. 1994 Jul 19;33(28):8453-63 Authors: Zink T, Ross A, Lüers K, Cieslar C, Rudolph R, Holak TA Recombinant 15N- and 13C-labeled human granulocyte colony-stimulating factor (rh-metG-CSF) has been studied by 2D and 3D...	nmrlearner	Journal club	0	08-22-2010 03:29 AM
[NMR paper] Characterization of the three-dimensional solution structure of human profilin: 1H, 1 Characterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern. Related Articles Characterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern. Biochemistry. 1993 Dec 21;32(50):13818-29 Authors: Metzler WJ, Constantine KL, Friedrichs MS, Bell AJ, Ernst EG, Lavoie TB, Mueller L Human profilin is a 15-kDa protein that plays a major role in the signaling pathway leading to cytoskeletal...	nmrlearner	Journal club	0	08-22-2010 03:01 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