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1cfp

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[[Image:1cfp.gif|left|200px]]
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{{STRUCTURE_1cfp| PDB=1cfp | SCENE= }}
{{STRUCTURE_1cfp| PDB=1cfp | SCENE= }}
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'''S100B (S100BETA) NMR DATA WAS COLLECTED FROM A SAMPLE OF CALCIUM FREE PROTEIN AT PH 6.3 AND A TEMPERATURE OF 311 K AND 1.7-6.9 MM CONCENTRATION, 25 STRUCTURES'''
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===S100B (S100BETA) NMR DATA WAS COLLECTED FROM A SAMPLE OF CALCIUM FREE PROTEIN AT PH 6.3 AND A TEMPERATURE OF 311 K AND 1.7-6.9 MM CONCENTRATION, 25 STRUCTURES===
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==Overview==
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BACKGROUND. S100B (S100beta) is a member of the S100 family of small calcium-binding proteins: members of this family contain two helix-loop-helix calcium-binding motifs and interact with a wide range of proteins involved mainly in the cytoskeleton and cell proliferation. S100B is a neurite-extension factor and levels of S100B are elevated in the brains of patients with Alzheimer's disease or Down's syndrome: the pattern of S100B overexpression in Alzheimer's disease correlates with the pattern of neuritic-plaque formation. Identification of a growing class of S100 proteins and the likely neurochemical importance of S100B make the determination of the structure of S100B of interest. RESULTS. We have used NMR to determine the structure of the reduced S100B homodimer in the absence of calcium. Each monomer consists of a four-helix bundle, arranged in the dimer in an antiparallel fashion. The fourth helix of each monomer runs close to the equivalent helix of the other monomer for almost its full length, extending the hydrophobic core through the interface. The N-terminal, but not the C-terminal, calcium-binding loop is similar to the equivalent loop in the monomeric S100 protein calbindin and is in a conformation ready to bind calcium. CONCLUSIONS. The novel dimer structure reported previously for calcyclin (S100A6) is the common fold for the dimeric S100B proteins. Calcium binding to the C-terminal calcium-binding loop would be expected to require a conformational change, which might provide a signal for activation. The structure suggests regions of the molecule likely to be involved in interactions with effector molecules.
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{{ABSTRACT_PUBMED_8805590}}
==About this Structure==
==About this Structure==
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1CFP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CFP OCA].
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1CFP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CFP OCA].
==Reference==
==Reference==
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[[Category: Calcium-binding protein]]
[[Category: Calcium-binding protein]]
[[Category: Helix-loop-helix]]
[[Category: Helix-loop-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:41:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:41:18 2008''

Revision as of 17:41, 30 June 2008

Image:1cfp.png

Template:STRUCTURE 1cfp

S100B (S100BETA) NMR DATA WAS COLLECTED FROM A SAMPLE OF CALCIUM FREE PROTEIN AT PH 6.3 AND A TEMPERATURE OF 311 K AND 1.7-6.9 MM CONCENTRATION, 25 STRUCTURES

Template:ABSTRACT PUBMED 8805590

About this Structure

1CFP is a Single protein structure of sequence from Bos taurus. Full experimental information is available from OCA.

Reference

The solution structure of the bovine S100B protein dimer in the calcium-free state., Kilby PM, Van Eldik LJ, Roberts GC, Structure. 1996 Sep 15;4(9):1041-52. PMID:8805590

Page seeded by OCA on Mon Jun 30 20:41:18 2008

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