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1nsh
From Proteopedia
(New page: 200px<br /><applet load="1nsh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nsh" /> '''Solution Structure of Rabbit apo-S100A11 (19...) |
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| - | [[Image:1nsh.gif|left|200px]]<br /><applet load="1nsh" size=" | + | [[Image:1nsh.gif|left|200px]]<br /><applet load="1nsh" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Solution Structure of Rabbit apo-S100A11 (19 models)'''<br /> | '''Solution Structure of Rabbit apo-S100A11 (19 models)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | S100A11 is a homodimeric EF-hand calcium binding protein that undergoes a | + | 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== | ||
| - | 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:// | + | 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]] | ||
| - | [[Category: Dempsey, A | + | [[Category: Dempsey, A C.]] |
| - | [[Category: Shaw, G | + | [[Category: Shaw, G S.]] |
| - | [[Category: Walsh, M | + | [[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]] | ||
| - | ''Page seeded by [http:// | + | ''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
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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
Page seeded by OCA on Thu Feb 21 14:09:30 2008
