1fjr

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(New page: 200px<br /><applet load="1fjr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fjr, resolution 2.30&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1fjr.jpg|left|200px]]<br /><applet load="1fjr" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1fjr.jpg|left|200px]]<br /><applet load="1fjr" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1fjr, resolution 2.30&Aring;" />
caption="1fjr, resolution 2.30&Aring;" />
'''CRYSTAL STRUCTURE OF THE ECTODOMAIN OF METHUSELAH'''<br />
'''CRYSTAL STRUCTURE OF THE ECTODOMAIN OF METHUSELAH'''<br />
==Overview==
==Overview==
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The Drosophila mutant methuselah (mth) was identified from a screen for, single gene mutations that extended average lifespan. Mth mutants have a, 35% increase in average lifespan and increased resistance to several forms, of stress, including heat, starvation, and oxidative damage. The protein, affected by this mutation is related to G protein-coupled receptors of the, secretin receptor family. Mth, like secretin receptor family members, has, a large N-terminal ectodomain, which may constitute the ligand binding, site. Here we report the 2.3-A resolution crystal structure of the Mth, extracellular region, revealing a folding topology in which three, primarily beta-structure-containing domains meet to form a shallow, interdomain groove containing a solvent-exposed tryptophan that may, represent a ligand binding site. The Mth structure is analyzed in relation, to predicted Mth homologs and potential ligand binding features.
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The Drosophila mutant methuselah (mth) was identified from a screen for single gene mutations that extended average lifespan. Mth mutants have a 35% increase in average lifespan and increased resistance to several forms of stress, including heat, starvation, and oxidative damage. The protein affected by this mutation is related to G protein-coupled receptors of the secretin receptor family. Mth, like secretin receptor family members, has a large N-terminal ectodomain, which may constitute the ligand binding site. Here we report the 2.3-A resolution crystal structure of the Mth extracellular region, revealing a folding topology in which three primarily beta-structure-containing domains meet to form a shallow interdomain groove containing a solvent-exposed tryptophan that may represent a ligand binding site. The Mth structure is analyzed in relation to predicted Mth homologs and potential ligand binding features.
==About this Structure==
==About this Structure==
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1FJR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with NAG, SO4 and PB as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FJR OCA].
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1FJR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=PB:'>PB</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FJR OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Benzer, S.]]
[[Category: Benzer, S.]]
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[[Category: Bjorkman, P.J.]]
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[[Category: Bjorkman, P J.]]
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[[Category: Jr., A.P.West.]]
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[[Category: Jr., A P.West.]]
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[[Category: Llamas, L.L.]]
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[[Category: Llamas, L L.]]
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[[Category: Snow, P.M.]]
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[[Category: Snow, P M.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: PB]]
[[Category: PB]]
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[[Category: gpcr]]
[[Category: gpcr]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:59:08 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:39:22 2008''

Revision as of 10:39, 21 February 2008


1fjr, resolution 2.30Å

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CRYSTAL STRUCTURE OF THE ECTODOMAIN OF METHUSELAH

Overview

The Drosophila mutant methuselah (mth) was identified from a screen for single gene mutations that extended average lifespan. Mth mutants have a 35% increase in average lifespan and increased resistance to several forms of stress, including heat, starvation, and oxidative damage. The protein affected by this mutation is related to G protein-coupled receptors of the secretin receptor family. Mth, like secretin receptor family members, has a large N-terminal ectodomain, which may constitute the ligand binding site. Here we report the 2.3-A resolution crystal structure of the Mth extracellular region, revealing a folding topology in which three primarily beta-structure-containing domains meet to form a shallow interdomain groove containing a solvent-exposed tryptophan that may represent a ligand binding site. The Mth structure is analyzed in relation to predicted Mth homologs and potential ligand binding features.

About this Structure

1FJR is a Single protein structure of sequence from Drosophila melanogaster with , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the ectodomain of Methuselah, a Drosophila G protein-coupled receptor associated with extended lifespan., West AP Jr, Llamas LL, Snow PM, Benzer S, Bjorkman PJ, Proc Natl Acad Sci U S A. 2001 Mar 27;98(7):3744-9. Epub 2001 Mar 13. PMID:11274391

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