1e0l
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1e0l.gif|left|200px]] | + | [[Image:1e0l.gif|left|200px]] |
| - | + | ||
| - | '''FBP28WW DOMAIN FROM MUS MUSCULUS''' | + | {{Structure |
| + | |PDB= 1e0l |SIZE=350|CAPTION= <scene name='initialview01'>1e0l</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''FBP28WW DOMAIN FROM MUS MUSCULUS''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1E0L is a [ | + | 1E0L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0L OCA]. |
==Reference== | ==Reference== | ||
| - | Structural analysis of WW domains and design of a WW prototype., Macias MJ, Gervais V, Civera C, Oschkinat H, Nat Struct Biol. 2000 May;7(5):375-9. PMID:[http:// | + | Structural analysis of WW domains and design of a WW prototype., Macias MJ, Gervais V, Civera C, Oschkinat H, Nat Struct Biol. 2000 May;7(5):375-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10802733 10802733] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 21: | Line 30: | ||
[[Category: ww domain]] | [[Category: ww domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:47:33 2008'' |
Revision as of 08:47, 20 March 2008
| |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
FBP28WW DOMAIN FROM MUS MUSCULUS
Overview
Two new NMR structures of WW domains, the mouse formin binding protein and a putative 84.5 kDa protein from Saccharomyces cerevisiae, show that this domain, only 35 amino acids in length, defines the smallest monomeric triple-stranded antiparallel beta-sheet protein domain that is stable in the absence of disulfide bonds, tightly bound ions or ligands. The structural roles of conserved residues have been studied using site-directed mutagenesis of both wild type domains. Crucial interactions responsible for the stability of the WW structure have been identified. Based on a network of highly conserved long range interactions across the beta-sheet structure that supports the WW fold and on a systematic analysis of conserved residues in the WW family, we have designed a folded prototype WW sequence.
About this Structure
1E0L is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural analysis of WW domains and design of a WW prototype., Macias MJ, Gervais V, Civera C, Oschkinat H, Nat Struct Biol. 2000 May;7(5):375-9. PMID:10802733
Page seeded by OCA on Thu Mar 20 10:47:33 2008
