1b4c
From Proteopedia
(New page: 200px<br /><applet load="1b4c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b4c" /> '''SOLUTION STRUCTURE OF RAT APO-S100B USING DI...) |
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'''SOLUTION STRUCTURE OF RAT APO-S100B USING DIPOLAR COUPLINGS'''<br /> | '''SOLUTION STRUCTURE OF RAT APO-S100B USING DIPOLAR COUPLINGS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The relative orientations of adjacent structural elements without many | + | The relative orientations of adjacent structural elements without many well-defined NOE contacts between them are typically poorly defined in NMR structures. For apo-S100B(betabeta) and the structurally homologous protein calcyclin, the solution structures determined by conventional NMR exhibited considerable differences and made it impossible to draw unambiguous conclusions regarding the Ca2+-induced conformational change required for target protein binding. The structure of rat apo-S100B(betabeta) was recalculated using a large number of constraints derived from dipolar couplings that were measured in a dilute liquid crystalline phase. The dipolar couplings orient bond vectors relative to a single-axis system, and thereby remove much of the uncertainty in NOE-based structures. The structure of apo-S100B(betabeta) indicates a minimal change in the first, pseudo-EF-hand Ca2+ binding site, but a large reorientation of helix 3 in the second, classical EF-hand upon Ca2+ binding. |
==About this Structure== | ==About this Structure== | ||
| - | 1B4C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1B4C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B4C OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Baldisseri, D | + | [[Category: Baldisseri, D M.]] |
| - | [[Category: Drohat, A | + | [[Category: Drohat, A C.]] |
[[Category: Tjandra, N.]] | [[Category: Tjandra, N.]] | ||
| - | [[Category: Weber, D | + | [[Category: Weber, D J.]] |
[[Category: calcium- binding protein]] | [[Category: calcium- binding protein]] | ||
[[Category: dipolar couplings]] | [[Category: dipolar couplings]] | ||
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[[Category: three-dimensional structure]] | [[Category: three-dimensional structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:51:20 2008'' |
Revision as of 09:51, 21 February 2008
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SOLUTION STRUCTURE OF RAT APO-S100B USING DIPOLAR COUPLINGS
Overview
The relative orientations of adjacent structural elements without many well-defined NOE contacts between them are typically poorly defined in NMR structures. For apo-S100B(betabeta) and the structurally homologous protein calcyclin, the solution structures determined by conventional NMR exhibited considerable differences and made it impossible to draw unambiguous conclusions regarding the Ca2+-induced conformational change required for target protein binding. The structure of rat apo-S100B(betabeta) was recalculated using a large number of constraints derived from dipolar couplings that were measured in a dilute liquid crystalline phase. The dipolar couplings orient bond vectors relative to a single-axis system, and thereby remove much of the uncertainty in NOE-based structures. The structure of apo-S100B(betabeta) indicates a minimal change in the first, pseudo-EF-hand Ca2+ binding site, but a large reorientation of helix 3 in the second, classical EF-hand upon Ca2+ binding.
About this Structure
1B4C is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
The use of dipolar couplings for determining the solution structure of rat apo-S100B(betabeta)., Drohat AC, Tjandra N, Baldisseri DM, Weber DJ, Protein Sci. 1999 Apr;8(4):800-9. PMID:10211826
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