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1nsh
From Proteopedia
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| - | [[Image:1nsh.gif|left|200px]] | + | [[Image:1nsh.gif|left|200px]] |
| - | + | ||
| - | '''Solution Structure of Rabbit apo-S100A11 (19 models)''' | + | {{Structure |
| + | |PDB= 1nsh |SIZE=350|CAPTION= <scene name='initialview01'>1nsh</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= S100A11 OR S100C OR PCALG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 Oryctolagus cuniculus]) | ||
| + | }} | ||
| + | |||
| + | '''Solution Structure of Rabbit apo-S100A11 (19 models)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1NSH is a [ | + | 1NSH is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12842051 12842051] |
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: s100a11]] | [[Category: s100a11]] | ||
| - | ''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 13:01:05 2008'' |
Revision as of 11:01, 20 March 2008
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| Gene: | S100A11 OR S100C OR PCALG (Oryctolagus cuniculus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mar 20 13:01:05 2008
