1fjr: Difference between revisions

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[[Image:1fjr.jpg|left|200px]]
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{{STRUCTURE_1fjr|  PDB=1fjr  |  SCENE=  }}  
{{STRUCTURE_1fjr|  PDB=1fjr  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE ECTODOMAIN OF METHUSELAH'''
===CRYSTAL STRUCTURE OF THE ECTODOMAIN OF METHUSELAH===




==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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{{ABSTRACT_PUBMED_11274391}}


==About this Structure==
==About this Structure==
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[[Category: G protein-coupled receptor]]
[[Category: G protein-coupled receptor]]
[[Category: Gpcr]]
[[Category: Gpcr]]
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Revision as of 00:22, 1 July 2008

File:1fjr.png

Template:STRUCTURE 1fjr

CRYSTAL STRUCTURE OF THE ECTODOMAIN OF METHUSELAH

Template:ABSTRACT PUBMED 11274391

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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