1fjr
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1fjr |SIZE=350|CAPTION= <scene name='initialview01'>1fjr</scene>, resolution 2.30Å | |PDB= 1fjr |SIZE=350|CAPTION= <scene name='initialview01'>1fjr</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fjr OCA], [http://www.ebi.ac.uk/pdbsum/1fjr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fjr RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Llamas, L L.]] | [[Category: Llamas, L L.]] | ||
[[Category: Snow, P M.]] | [[Category: Snow, P M.]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: PB]] | ||
| - | [[Category: SO4]] | ||
[[Category: ectodomain]] | [[Category: ectodomain]] | ||
[[Category: g protein-coupled receptor]] | [[Category: g protein-coupled receptor]] | ||
[[Category: gpcr]] | [[Category: gpcr]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:24:15 2008'' |
Revision as of 17:24, 30 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Sun Mar 30 20:24:15 2008
