1nsh | pdb_00001nsh
Solution Structure of Rabbit apo-S100A11 (19 models)
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| 1nsh | |||||||||||||
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| Gene: | S100A11 OR S100C OR PCALG (Oryctolagus cuniculus) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
