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1ytv

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(New page: 200px<br /> <applet load="1ytv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ytv, resolution 1.80&Aring;" /> '''Maltose-binding pro...)
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[[Image:1ytv.gif|left|200px]]<br />
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[[Image:1ytv.gif|left|200px]]<br /><applet load="1ytv" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1ytv" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1ytv, resolution 1.80&Aring;" />
caption="1ytv, resolution 1.80&Aring;" />
'''Maltose-binding protein fusion to a C-terminal fragment of the V1a vasopressin receptor'''<br />
'''Maltose-binding protein fusion to a C-terminal fragment of the V1a vasopressin receptor'''<br />
==Overview==
==Overview==
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The V1 vascular vasopressin receptor (V1R) is a G-protein-coupled receptor, (GPCR) involved in the regulation of body-fluid osmolality, blood volume, and blood pressure. Signal transduction is mediated by the third, intracellular loop of this seven-transmembrane protein as well as by the, C-terminal cytoplasmic segment. A chimera of the maltose-binding protein, (MBP) and the C-terminal segment of V1R has been cloned, expressed, purified and crystallized. The crystals belong to space group P2(1), with, unit-cell parameters a = 51.10, b = 66.56, c = 115.72 A, beta = 95.99, degrees. The 1.8 A crystal structure reveals the conformation of MBP and, part of the linker region of this chimera, with the C-terminal segment, being unstructured. This may reflect a conformational plasticity in the, C-terminal segment that may be necessary for proper function of V1R.
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The V1 vascular vasopressin receptor (V1R) is a G-protein-coupled receptor (GPCR) involved in the regulation of body-fluid osmolality, blood volume and blood pressure. Signal transduction is mediated by the third intracellular loop of this seven-transmembrane protein as well as by the C-terminal cytoplasmic segment. A chimera of the maltose-binding protein (MBP) and the C-terminal segment of V1R has been cloned, expressed, purified and crystallized. The crystals belong to space group P2(1), with unit-cell parameters a = 51.10, b = 66.56, c = 115.72 A, beta = 95.99 degrees. The 1.8 A crystal structure reveals the conformation of MBP and part of the linker region of this chimera, with the C-terminal segment being unstructured. This may reflect a conformational plasticity in the C-terminal segment that may be necessary for proper function of V1R.
==About this Structure==
==About this Structure==
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1YTV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MAL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YTV OCA].
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1YTV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MAL:'>MAL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YTV OCA].
==Reference==
==Reference==
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A C-terminal segment of the V1R vasopressin receptor is unstructured in the crystal structure of its chimera with the maltose-binding protein., Adikesavan NV, Mahmood SS, Stanley N, Xu Z, Wu N, Thibonnier M, Shoham M, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2005 Apr 1;61(Pt, 4):341-5. Epub 2005 Mar 24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16511036 16511036]
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A C-terminal segment of the V1R vasopressin receptor is unstructured in the crystal structure of its chimera with the maltose-binding protein., Adikesavan NV, Mahmood SS, Stanley N, Xu Z, Wu N, Thibonnier M, Shoham M, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Apr 1;61(Pt, 4):341-5. Epub 2005 Mar 24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16511036 16511036]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Adikesavan, N.V]]
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[[Category: Adikesavan, N V]]
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[[Category: Mahmood, S.S.]]
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[[Category: Mahmood, S S.]]
[[Category: Shoham, M.]]
[[Category: Shoham, M.]]
[[Category: Stanley,, S.]]
[[Category: Stanley,, S.]]
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[[Category: vasopressin; receptor; gpcr; fusion protein; maltose-binding protein]]
[[Category: vasopressin; receptor; gpcr; fusion protein; maltose-binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:24:33 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:09:02 2008''

Revision as of 14:09, 21 February 2008


1ytv, resolution 1.80Å

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Maltose-binding protein fusion to a C-terminal fragment of the V1a vasopressin receptor

Overview

The V1 vascular vasopressin receptor (V1R) is a G-protein-coupled receptor (GPCR) involved in the regulation of body-fluid osmolality, blood volume and blood pressure. Signal transduction is mediated by the third intracellular loop of this seven-transmembrane protein as well as by the C-terminal cytoplasmic segment. A chimera of the maltose-binding protein (MBP) and the C-terminal segment of V1R has been cloned, expressed, purified and crystallized. The crystals belong to space group P2(1), with unit-cell parameters a = 51.10, b = 66.56, c = 115.72 A, beta = 95.99 degrees. The 1.8 A crystal structure reveals the conformation of MBP and part of the linker region of this chimera, with the C-terminal segment being unstructured. This may reflect a conformational plasticity in the C-terminal segment that may be necessary for proper function of V1R.

About this Structure

1YTV is a Protein complex structure of sequences from Escherichia coli and Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

A C-terminal segment of the V1R vasopressin receptor is unstructured in the crystal structure of its chimera with the maltose-binding protein., Adikesavan NV, Mahmood SS, Stanley N, Xu Z, Wu N, Thibonnier M, Shoham M, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Apr 1;61(Pt, 4):341-5. Epub 2005 Mar 24. PMID:16511036

Page seeded by OCA on Thu Feb 21 16:09:02 2008

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