1fjr: Difference between revisions
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[[Image:1fjr.jpg|left|200px]] | [[Image:1fjr.jpg|left|200px]] | ||
'''CRYSTAL STRUCTURE OF THE ECTODOMAIN OF METHUSELAH''' | {{Structure | ||
|PDB= 1fjr |SIZE=350|CAPTION= <scene name='initialview01'>1fjr</scene>, resolution 2.30Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=PB:LEAD (II) ION'>PB</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF THE ECTODOMAIN OF METHUSELAH''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1FJR is a [ | 1FJR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FJR OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11274391 11274391] | ||
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: gpcr]] | [[Category: gpcr]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:10:04 2008'' | ||
Revision as of 09:10, 20 March 2008
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| 1fjr, resolution 2.30Å | |||||||||||||
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| Ligands: | NAG, SO4 and PB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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