1mho: Difference between revisions

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[[Image:1mho.jpg|left|200px]]<br /><applet load="1mho" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1mho.jpg|left|200px]]<br /><applet load="1mho" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1mho, resolution 2.0Å" />

'''THE 2.0 A STRUCTURE OF HOLO S100B FROM BOVINE BRAIN'''<br />

==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.

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==

1MHO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1MHO OCA].

1MHO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MHO OCA].

==Reference==

Line 17:

[[Category: Matsumura, H.]]

[[Category: Shiba, T.]]

[[Category: Yasushi, K.A.I.]]

[[Category: Yasushi, K A.I.]]

[[Category: CA]]

[[Category: acetylation]]

Line 24:

[[Category: zinc]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:55:17 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1mho.jpg|left|200px]]<br /><applet load="1mho" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1mho.jpg|left|200px]]<br /><applet load="1mho" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1mho, resolution 2.0&Aring;" />
 '''THE 2.0 A STRUCTURE OF HOLO S100B FROM BOVINE BRAIN'''<br />
 ==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.
+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==
-MHO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MHO OCA].
+MHO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MHO OCA].
 ==Reference==
@@ Line 17: / Line 17: @@
 [[Category: Matsumura, H.]]
 [[Category: Shiba, T.]]
-[[Category: Yasushi, K.A.I.]]
+[[Category: Yasushi, K A.I.]]
 [[Category: CA]]
 [[Category: acetylation]]
@@ Line 24: / Line 24: @@
 [[Category: zinc]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:25:24 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:55:17 2008''