2k0p: Difference between revisions

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     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2k0p ConSurf].
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Revision as of 18:58, 9 February 2016

Determination of a Protein Structure in the Solid State from NMR Chemical ShiftsDetermination of a Protein Structure in the Solid State from NMR Chemical Shifts

Structural highlights

2k0p is a 1 chain structure with sequence from Streptococcus sp. group g. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:spg (Streptococcus sp. group G)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[SPG1_STRSG] Binds to the constant Fc region of IgG with high affinity.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Solid-state NMR spectroscopy does not require proteins to form crystalline or soluble samples and can thus be applied under a variety of conditions, including precipitates, gels, and microcrystals. It has recently been shown that NMR chemical shifts can be used to determine the structures of the native states of proteins in solution. By considering the cases of two proteins, GB1 and SH3, we provide an initial demonstration here that this type of approach can be extended to the use of solid-state NMR chemical shifts to obtain protein structures in the solid state without the need for measuring interatomic distances.

Determination of protein structures in the solid state from NMR chemical shifts.,Robustelli P, Cavalli A, Vendruscolo M Structure. 2008 Dec 10;16(12):1764-9. PMID:19081052[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Robustelli P, Cavalli A, Vendruscolo M. Determination of protein structures in the solid state from NMR chemical shifts. Structure. 2008 Dec 10;16(12):1764-9. PMID:19081052 doi:10.1016/j.str.2008.10.016
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