1e0m: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1e0m.gif|left|200px]] | [[Image:1e0m.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1e0m", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
| | or leave the SCENE parameter empty for the default display. | ||
| | --> | ||
{{STRUCTURE_1e0m| PDB=1e0m | SCENE= }} | |||
}} | |||
'''PROTOTYPE WW DOMAIN''' | '''PROTOTYPE WW DOMAIN''' | ||
| Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0M 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://www.ncbi.nlm.nih.gov/pubmed/10802733 10802733] | 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: Civera, C.]] | [[Category: Civera, C.]] | ||
[[Category: Gervais, V.]] | [[Category: Gervais, V.]] | ||
[[Category: Macias, M J.]] | [[Category: Macias, M J.]] | ||
[[Category: Oschkinat, H.]] | [[Category: Oschkinat, H.]] | ||
[[Category: | [[Category: Protein design]] | ||
[[Category: | [[Category: Wwprototype]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:30:45 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 11:30, 2 May 2008
PROTOTYPE WW DOMAIN
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
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 Fri May 2 14:30:45 2008