1uwo
From Proteopedia
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| - | [[Image:1uwo.jpg|left|200px]]< | + | [[Image:1uwo.jpg|left|200px]] |
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| - | '''CALCIUM FORM OF HUMAN S100B, NMR, 20 STRUCTURES''' | + | {{Structure |
| + | |PDB= 1uwo |SIZE=350|CAPTION= <scene name='initialview01'>1uwo</scene> | ||
| + | |SITE= <scene name='pdbsite=CA1:Pseudo+Ef-Hand+Ca-Binding+Site+Monomer+A'>CA1</scene>, <scene name='pdbsite=CA2:Canonical+Ef-Hand+Ca-Binding+Site+Monomer+A'>CA2</scene>, <scene name='pdbsite=CA3:Pseudo+Ef-Hand+Ca-Binding+Site+Monomer+B'>CA3</scene> and <scene name='pdbsite=CA4:Canonical+Ef-Hand+Ca-Binding+Site+Monomer+B'>CA4</scene> | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CALCIUM FORM OF HUMAN S100B, NMR, 20 STRUCTURES''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UWO is a [ | + | 1UWO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UWO OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9519411 9519411] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: solution structure]] | [[Category: solution structure]] | ||
| - | ''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 14:37:51 2008'' |
Revision as of 12:37, 20 March 2008
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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
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