1cfp
From Proteopedia
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==Overview== | ==Overview== | ||
| - | 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, ... | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1CFP is a | + | 1CFP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Structure known Active Sites: LOA, LOB, LOC and LOD. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CFP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: helix-loop-helix]] | [[Category: helix-loop-helix]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:38:42 2007'' |
Revision as of 10:33, 5 November 2007
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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
Overview
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.
About this Structure
1CFP is a Single protein structure of sequence from Bos taurus. Structure known Active Sites: LOA, LOB, LOC and LOD. Full crystallographic 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 Nov 5 12:38:42 2007
