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1fjr
From Proteopedia
(New page: 200px<br /><applet load="1fjr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fjr, resolution 2.30Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1fjr.jpg|left|200px]]<br /><applet load="1fjr" size=" | + | [[Image:1fjr.jpg|left|200px]]<br /><applet load="1fjr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fjr, resolution 2.30Å" /> | caption="1fjr, resolution 2.30Å" /> | ||
'''CRYSTAL STRUCTURE OF THE ECTODOMAIN OF METHUSELAH'''<br /> | '''CRYSTAL STRUCTURE OF THE ECTODOMAIN OF METHUSELAH'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Drosophila mutant methuselah (mth) was identified from a screen for | + | 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== | ||
| - | 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:// | + | 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.]] | ||
| - | [[Category: Bjorkman, P | + | [[Category: Bjorkman, P J.]] |
| - | [[Category: Jr., A | + | [[Category: Jr., A P.West.]] |
| - | [[Category: Llamas, L | + | [[Category: Llamas, L L.]] |
| - | [[Category: Snow, P | + | [[Category: Snow, P M.]] |
[[Category: NAG]] | [[Category: NAG]] | ||
[[Category: PB]] | [[Category: PB]] | ||
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[[Category: gpcr]] | [[Category: gpcr]] | ||
| - | ''Page seeded by [http:// | + | ''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
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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
Page seeded by OCA on Thu Feb 21 12:39:22 2008
