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 2.30Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 12:51, 20 November 2007
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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 NAG, SO4 and PB 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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