1fjr
From Proteopedia
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'''CRYSTAL STRUCTURE OF THE ECTODOMAIN OF METHUSELAH''' | '''CRYSTAL STRUCTURE OF THE ECTODOMAIN OF METHUSELAH''' | ||
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[[Category: Llamas, L L.]] | [[Category: Llamas, L L.]] | ||
[[Category: Snow, P M.]] | [[Category: Snow, P M.]] | ||
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| - | [[Category: | + | [[Category: G protein-coupled receptor]] |
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:24:40 2008'' | |
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Revision as of 13:24, 2 May 2008
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 Page seeded by OCA on Fri May 2 16:24:40 2008
