NMR paper High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensio

		BioNMR > Educational resources > Journal club
[NMR paper] High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensio

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, 03:33 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

High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensio

High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR.

Related Articles High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR.

Science. 1994 Mar 25;263(5154):1762-7

Authors: Lodi PJ, Garrett DS, Kuszewski J, Tsang ML, Weatherbee JA, Leonard WJ, Gronenborn AM, Clore GM

The three-dimensional structure of a member of the beta subfamily of chemokines, human macrophage inflammatory protein-1 beta (hMIP-1 beta), has been determined with the use of solution multidimensional heteronuclear magnetic resonance spectroscopy. Human MIP-1 beta is a symmetric homodimer with a relative molecular mass of approximately 16 kilodaltons. The structure of the hMIP-1 beta monomer is similar to that of the related alpha chemokine interleukin-8 (IL-8). However, the quaternary structures of the two proteins are entirely distinct, and the dimer interface is formed by a completely different set of residues. Whereas the IL-8 dimer is globular, the hMIP-1 beta dimer is elongated and cylindrical. This provides a rational explanation for the absence of cross-binding and reactivity between the alpha and beta chemokine subfamilies. Calculation of the solvation free energies of dimerization suggests that the formation and stabilization of the two different types of dimers arise from the burial of hydrophobic residues.

PMID: 8134838 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Characterization of amyloid fibrils of human beta-2-microglobulin by high-resolution magic-angle spinning NMR. Characterization of amyloid fibrils of human beta-2-microglobulin by high-resolution magic-angle spinning NMR. Characterization of amyloid fibrils of human beta-2-microglobulin by high-resolution magic-angle spinning NMR. Chembiochem. 2010 Sep 3;11(13):1829-32 Authors: Skora L, Becker S, Zweckstetter M	nmrlearner	Journal club	0	01-05-2011 09:51 PM
[NMR paper] alpha-->beta transition of beta-lactoglobulin as evidenced by heteronuclear NMR. alpha-->beta transition of beta-lactoglobulin as evidenced by heteronuclear NMR. Related Articles alpha-->beta transition of beta-lactoglobulin as evidenced by heteronuclear NMR. J Mol Biol. 1998 Nov 6;283(4):731-9 Authors: Kuwata K, Hoshino M, Era S, Batt CA, Goto Y Whereas bovine beta-lactoglobulin is a predominantly beta-sheet protein, it has a marked alpha-helical preference and can be considered to be a useful model of the alpha-->beta transition, a key issue for understanding the folding and biological function of a number of proteins....	nmrlearner	Journal club	0	11-17-2010 11:15 PM
[NMR paper] High-resolution solution NMR structure of the Z domain of staphylococcal protein A. High-resolution solution NMR structure of the Z domain of staphylococcal protein A. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles High-resolution solution NMR structure of the Z domain of staphylococcal protein A. J Mol Biol. 1997 Oct 3;272(4):573-90 Authors: Tashiro M, Tejero R, Zimmerman DE, Celda B, Nilsson B, Montelione GT Staphylococcal protein A (SpA) is a cell-wall-bound pathogenicity factor from the bacterium Staphylococcus aureus. Because of their small size...	nmrlearner	Journal club	0	08-22-2010 05:08 PM
[NMR paper] High helicity of peptide fragments corresponding to beta-strand regions of beta-lacto High helicity of peptide fragments corresponding to beta-strand regions of beta-lactoglobulin observed by 2D-NMR spectroscopy. Related Articles High helicity of peptide fragments corresponding to beta-strand regions of beta-lactoglobulin observed by 2D-NMR spectroscopy. Fold Des. 1996;1(4):255-63 Authors: Kuroda Y, Hamada D, Tanaka T, Goto Y BACKGROUND: Whereas protein fragments, when they are structured, adopt conformations similar to that found in the native state, the high helical propensity of beta-lactoglobulin, a predominantly beta-sheet...	nmrlearner	Journal club	0	08-22-2010 02:27 PM
[NMR paper] Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy. Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy. Biochemistry. 1996 Sep 10;35(36):11577-88 Authors: Drohat AC, Amburgey JC, Abildgaard F, Starich MR, Baldisseri D, Weber DJ S100B(beta beta), a member of the S100 protein family, is a Ca(2+)-binding protein with noncovalent interactions at its dimer interface. Each apo-S100 beta...	nmrlearner	Journal club	0	08-22-2010 02:20 PM
[NMR paper] High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensio High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR. Related Articles High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR. Science. 1994 Mar 25;263(5154):1762-7 Authors: Lodi PJ, Garrett DS, Kuszewski J, Tsang ML, Weatherbee JA, Leonard WJ, Gronenborn AM, Clore GM The three-dimensional structure of a member of the beta subfamily of chemokines, human macrophage inflammatory protein-1 beta (hMIP-1 beta), has been determined with the use of solution multidimensional...	nmrlearner	Journal club	0	08-22-2010 03:33 AM
[NMR paper] 1H NMR assignments and secondary structure of human beta 2-microglobulin in solution. 1H NMR assignments and secondary structure of human beta 2-microglobulin in solution. Related Articles 1H NMR assignments and secondary structure of human beta 2-microglobulin in solution. Biochemistry. 1992 Sep 22;31(37):8906-15 Authors: Okon M, Bray P, VuceliÄ? D Sequence-specific resonance assignments of human beta 2-microglobulin (M(r) 12,000) and its secondary structure are determined by 2D NMR techniques. The protein is found to contain two antiparallel beta-sheets each of four beta-strands with the beta-sheets being connected by a...	nmrlearner	Journal club	0	08-21-2010 11:45 PM
[NMR paper] The solution conformation of tubulin-beta(422-434)-NH2 and its Nac-DATADEQG-NH2 fragm The solution conformation of tubulin-beta(422-434)-NH2 and its Nac-DATADEQG-NH2 fragment based on NMR. Related Articles The solution conformation of tubulin-beta(422-434)-NH2 and its Nac-DATADEQG-NH2 fragment based on NMR. Biopolymers. 1991 Mar;31(4):449-58 Authors: Otter A, Scott PG, Maccioni RB, Kotovych G The solution conformation of tubulin-beta(422-434)-NH2 (YQQYQDATADEQG-NH2) and its Nac-DATADEQG-NH2 fragment has been studied by two-dimensional 1H-nmr spectroscopy in CD3OH/H2O (90/10 v/v) at neutral and low pH. The 13 amino acid peptide...	nmrlearner	Journal club	0	08-21-2010 11:16 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