1u06
From Proteopedia
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| - | [[Image:1u06.gif|left|200px]] | + | [[Image:1u06.gif|left|200px]] |
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| - | '''crystal structure of chicken alpha-spectrin SH3 domain''' | + | {{Structure |
| + | |PDB= 1u06 |SIZE=350|CAPTION= <scene name='initialview01'>1u06</scene>, resolution 1.49Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=AZI:AZIDE ION'>AZI</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''crystal structure of chicken alpha-spectrin SH3 domain''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1U06 is a [ | + | 1U06 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U06 OCA]. |
==Reference== | ==Reference== | ||
| - | Detection of dynamic water molecules in a microcrystalline sample of the SH3 domain of alpha-spectrin by MAS solid-state NMR., Chevelkov V, Faelber K, Diehl A, Heinemann U, Oschkinat H, Reif B, J Biomol NMR. 2005 Apr;31(4):295-310. PMID:[http:// | + | Detection of dynamic water molecules in a microcrystalline sample of the SH3 domain of alpha-spectrin by MAS solid-state NMR., Chevelkov V, Faelber K, Diehl A, Heinemann U, Oschkinat H, Reif B, J Biomol NMR. 2005 Apr;31(4):295-310. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15928996 15928996] |
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: AZI]] | [[Category: AZI]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
| - | [[Category: five antiparallel beta | + | [[Category: five antiparallel beta sheet]] |
[[Category: sh3 domain]] | [[Category: sh3 domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:25:34 2008'' |
Revision as of 12:25, 20 March 2008
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| , resolution 1.49Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
crystal structure of chicken alpha-spectrin SH3 domain
Overview
Water molecules are a major determinant of protein stability and are important for understanding protein-protein interactions. We present two experiments which allow to measure first the effective T(2) decay rate of individual amide proton, and second the magnetization build-up rates for a selective transfer from H(2)O to H(N) using spin diffusion as a mixing element. The experiments are demonstrated for a uniformly (2)H, (15)N labeled sample of a microcrystalline SH3 domain in which exchangeable deuterons were back-substituted with protons. In order to evaluate the NMR experimental data, as X-ray structure of the protein was determined using the same crystallization protocol as for the solid-state NMR sample. The NMR experimental data are correlated with the dipolar couplings calculated from H(2)O-H(N) distances which were extracted from the X-ray structure of the protein. We find that the H(N) T(2) decay rates and H(2)O-H(N) build-up rates are sensitive to distance and dynamics of the detected water molecules with respect to the protein. We show that qualitative information about localization and dynamics of internal water molecules can be obtained in the solid-state by interpretation of the spin dynamics of a reporter amide proton.
About this Structure
1U06 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Detection of dynamic water molecules in a microcrystalline sample of the SH3 domain of alpha-spectrin by MAS solid-state NMR., Chevelkov V, Faelber K, Diehl A, Heinemann U, Oschkinat H, Reif B, J Biomol NMR. 2005 Apr;31(4):295-310. PMID:15928996
Page seeded by OCA on Thu Mar 20 14:25:34 2008
