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1nsh

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'''Solution Structure of Rabbit apo-S100A11 (19 models)'''<br />
'''Solution Structure of Rabbit apo-S100A11 (19 models)'''<br />
==Overview==
==Overview==
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S100A11 is a homodimeric EF-hand calcium binding protein that undergoes a, calcium-induced conformational change and interacts with the phospholipid, binding protein annexin I to coordinate membrane association. In this, work, the solution structure of apo-S100A11 has been determined by NMR, spectroscopy to uncover the details of its calcium-induced structural, change. Apo-S100A11 forms a tight globular structure having a near, antiparallel orientation of helices III and IV in calcium binding site II., Further, helices I and IV, and I and I', form a more closed arrangement, than observed in other apo-S100 proteins. This helix arrangement in, apo-S100A11 partially buries residues in helices I (P3, E11, A15), III, (V55, R58, M59), and IV (A86, C87, S90) and the linker (A45, F46), which, are required for interaction with annexin I in the calcium-bound state. In, apo-S100A11, this results in a "masked" binding surface that prevents, annexin I binding but is uncovered upon calcium binding.
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S100A11 is a homodimeric EF-hand calcium binding protein that undergoes a calcium-induced conformational change and interacts with the phospholipid binding protein annexin I to coordinate membrane association. In this work, the solution structure of apo-S100A11 has been determined by NMR spectroscopy to uncover the details of its calcium-induced structural change. Apo-S100A11 forms a tight globular structure having a near antiparallel orientation of helices III and IV in calcium binding site II. Further, helices I and IV, and I and I', form a more closed arrangement than observed in other apo-S100 proteins. This helix arrangement in apo-S100A11 partially buries residues in helices I (P3, E11, A15), III (V55, R58, M59), and IV (A86, C87, S90) and the linker (A45, F46), which are required for interaction with annexin I in the calcium-bound state. In apo-S100A11, this results in a "masked" binding surface that prevents annexin I binding but is uncovered upon calcium binding.
==About this Structure==
==About this Structure==
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1NSH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NSH OCA].
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1NSH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NSH OCA].
==Reference==
==Reference==
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[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Dempsey, A.C.]]
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[[Category: Dempsey, A C.]]
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[[Category: Shaw, G.S.]]
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[[Category: Shaw, G S.]]
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[[Category: Walsh, M.P.]]
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[[Category: Walsh, M P.]]
[[Category: calcium-binding protein]]
[[Category: calcium-binding protein]]
[[Category: ef hand]]
[[Category: ef hand]]
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[[Category: s100a11]]
[[Category: s100a11]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:31:24 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:09:30 2008''

Revision as of 12:09, 21 February 2008


1nsh

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Solution Structure of Rabbit apo-S100A11 (19 models)

Overview

S100A11 is a homodimeric EF-hand calcium binding protein that undergoes a calcium-induced conformational change and interacts with the phospholipid binding protein annexin I to coordinate membrane association. In this work, the solution structure of apo-S100A11 has been determined by NMR spectroscopy to uncover the details of its calcium-induced structural change. Apo-S100A11 forms a tight globular structure having a near antiparallel orientation of helices III and IV in calcium binding site II. Further, helices I and IV, and I and I', form a more closed arrangement than observed in other apo-S100 proteins. This helix arrangement in apo-S100A11 partially buries residues in helices I (P3, E11, A15), III (V55, R58, M59), and IV (A86, C87, S90) and the linker (A45, F46), which are required for interaction with annexin I in the calcium-bound state. In apo-S100A11, this results in a "masked" binding surface that prevents annexin I binding but is uncovered upon calcium binding.

About this Structure

1NSH is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

Unmasking the annexin I interaction from the structure of Apo-S100A11., Dempsey AC, Walsh MP, Shaw GS, Structure. 2003 Jul;11(7):887-97. PMID:12842051

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