1fjr: Difference between revisions

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[[Image:1fjr.~~jpg~~|left|200px]]

[[Image:1fjr.png|left|200px]]

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~~'''~~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.

The line below this paragraph, {{ABSTRACT_PUBMED_11274391}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11274391 is the PubMed ID number.

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==About this Structure==

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[[Category: G protein-coupled receptor]]

[[Category: Gpcr]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 16~~:24:40 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:22:29 2008''

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-[[Image:1fjr.jpg|left|200px]]
+{{Seed}}
+[[Image:1fjr.png|left|200px]]
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 {{STRUCTURE_1fjr|  PDB=1fjr  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE ECTODOMAIN OF METHUSELAH'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11274391}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11274391 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11274391}}
 ==About this Structure==
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 [[Category: G protein-coupled receptor]]
 [[Category: Gpcr]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:24:40 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 03:22:29 2008''