1uwo
From Proteopedia
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'''CALCIUM FORM OF HUMAN S100B, NMR, 20 STRUCTURES''' | '''CALCIUM FORM OF HUMAN S100B, NMR, 20 STRUCTURES''' | ||
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[[Category: Shaw, G S.]] | [[Category: Shaw, G S.]] | ||
[[Category: Smith, S P.]] | [[Category: Smith, S P.]] | ||
| - | [[Category: | + | [[Category: Calcium-binding protein]] |
| - | [[Category: | + | [[Category: Conformational change]] |
| - | [[Category: | + | [[Category: Ef-hand]] |
| - | [[Category: | + | [[Category: Human s100b]] |
| - | [[Category: | + | [[Category: Nmr]] |
| - | [[Category: | + | [[Category: Solution structure]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:47:11 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 08:47, 3 May 2008
CALCIUM FORM OF HUMAN S100B, NMR, 20 STRUCTURES
Overview
BACKGROUND: S100B is a homodimeric member of the EF-hand calcium-binding protein superfamily. The protein has been implicated in cellular processes such as cell differentiation and growth, plays a role in cytoskeletal structure and function, and may have a role in neuropathological diseases, such as Alzheimers. The effects of S100B are mediated via its interaction with target proteins. While several studies have suggested that this interaction is propagated through a calcium-induced conformational change, leading to the exposure of a hydrophobic region of S100B, the molecular details behind this structural alteration remain unclear. RESULTS: The solution structure of calcium-saturated human S100B (Ca(2+)-S100B) has been determined by heteronuclear NMR spectroscopy. Ca(2+)-S100B forms a well defined globular structure comprising four EF-hand calcium-binding sites and an extensive hydrophobic dimer interface. A comparison of Ca(2+)-S100B with apo S100B and Ca(2+)-calbindin D9k indicates that while calcium-binding to S100B results in little change in the site I EF-hand, it induces a backbone reorientation of the N terminus of the site II EF-hand. This reorientation leads to a dramatic change in the position of helix III relative to the other helices. CONCLUSIONS: The calcium-induced reorientation of calcium-binding site II results in the increased exposure of several hydrophobic residues in helix IV and the linker region. While following the general mechanism of calcium modulatory proteins, whereby a hydrophobic target site is exposed, the 'calcium switch' observed in S100B appears to be unique from that of other EF-hand proteins and may provide insights into target specificity among calcium modulatory proteins.
About this Structure
1UWO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form., Smith SP, Shaw GS, Structure. 1998 Feb 15;6(2):211-22. PMID:9519411 Page seeded by OCA on Sat May 3 11:47:11 2008
