1c9h

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(New page: 200px<br /> <applet load="1c9h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c9h, resolution 2.00&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1c9h.gif|left|200px]]<br />
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[[Image:1c9h.gif|left|200px]]<br /><applet load="1c9h" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1c9h" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1c9h, resolution 2.00&Aring;" />
caption="1c9h, resolution 2.00&Aring;" />
'''CRYSTAL STRUCTURE OF FKBP12.6 IN COMPLEX WITH RAPAMYCIN'''<br />
'''CRYSTAL STRUCTURE OF FKBP12.6 IN COMPLEX WITH RAPAMYCIN'''<br />
==Overview==
==Overview==
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FKBP12.6 is a novel isoform of FKBP12, which selectively binds to the, cardiac ryanodine receptor (RyR2). The crystal structure of FKBP12.6 in, complex with rapamycin has now been determined at 2.0 A resolution. The, structures of FKBP12.6 and FKBP12 are nearly identical, except for a, displacement observed in the helical region of FKBP12.6 toward the, hydrophobic pocket. This displacement was not predicted by homology, modeling studies. Analyses of the residues that are likely to confer the, RyR2-binding specificity are presented.
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FKBP12.6 is a novel isoform of FKBP12, which selectively binds to the cardiac ryanodine receptor (RyR2). The crystal structure of FKBP12.6 in complex with rapamycin has now been determined at 2.0 A resolution. The structures of FKBP12.6 and FKBP12 are nearly identical, except for a displacement observed in the helical region of FKBP12.6 toward the hydrophobic pocket. This displacement was not predicted by homology modeling studies. Analyses of the residues that are likely to confer the RyR2-binding specificity are presented.
==About this Structure==
==About this Structure==
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1C9H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with RAP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C9H OCA].
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1C9H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=RAP:'>RAP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C9H OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Carson, M.]]
[[Category: Carson, M.]]
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[[Category: Chodavarapu, C.S.]]
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[[Category: Chodavarapu, C S.]]
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[[Category: Deivanayagam, C.C.S.]]
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[[Category: Deivanayagam, C C.S.]]
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[[Category: Narayana, S.V.L.]]
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[[Category: Narayana, S V.L.]]
[[Category: Thotakura, A.]]
[[Category: Thotakura, A.]]
[[Category: RAP]]
[[Category: RAP]]
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[[Category: ryanodine receptor]]
[[Category: ryanodine receptor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:18:40 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:03:47 2008''

Revision as of 10:03, 21 February 2008


1c9h, resolution 2.00Å

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CRYSTAL STRUCTURE OF FKBP12.6 IN COMPLEX WITH RAPAMYCIN

Overview

FKBP12.6 is a novel isoform of FKBP12, which selectively binds to the cardiac ryanodine receptor (RyR2). The crystal structure of FKBP12.6 in complex with rapamycin has now been determined at 2.0 A resolution. The structures of FKBP12.6 and FKBP12 are nearly identical, except for a displacement observed in the helical region of FKBP12.6 toward the hydrophobic pocket. This displacement was not predicted by homology modeling studies. Analyses of the residues that are likely to confer the RyR2-binding specificity are presented.

About this Structure

1C9H is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of FKBP12.6 in complex with rapamycin., Deivanayagam CC, Carson M, Thotakura A, Narayana SV, Chodavarapu RS, Acta Crystallogr D Biol Crystallogr. 2000 Mar;56(Pt 3):266-71. PMID:10713512

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