Talk:MAP2K7

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Changes made

I made important edits to many sub-sections. It is all about the wording: the difference between motif (= an intrinsically disordered peptide segment that only becomes ordered once bound to its partner) and the domains (autonomously folding without any external binding partner) should be made clear. I agree, that even specialist articles tend to use sloppy wording; and authors often forget about these important differences. A special care is needed when addressing the DVD region: this is neither a domain, nor a motif, but falls into the structural category of a "domain extension". It is known for a while that nature rarely respects the functional boundaries when evolving novel domain architectures. Several domains come with extended folds, that give novel (additional) functionality to an old architecture. The DVD region found on MAP2Ks is a similar example. It can be seen on all X-ray structures determined so far, that it adds onto the back side of the catalytic core. Thus it works as a novel fold added onto the kinase domain. It is not a linear motif, since it is completely ordered in native proteins. So it is best called as a "region", to avoid confusion with "motifs" (disordered) and "domains" (stable/folding on their own). — Preceding unsigned comment added by Bubus (talk • contribs) 17:18, 29 December 2012 (UTC)[reply]

I have expanded the article with nomenclature, structure and function, signaling and regulation and have also rearranged the "interaction" section that was already there. By rearranging I mean changing the setup and also making the references more easy, with a shorter PMID-numbered reference. We re-wrote the first line from the old article, which made it hard to understand what was the gene and what was protein. A picture of the domains is also coming eventually. — Preceding unsigned comment added by Elisky89 (talk • contribs) 21:00, 10 April 2012 (UTC)[reply]

More headlines

Added "role in disease" and "isoforms" and will hopefully get the text in tomorrow. A picture of different domains are also coming. — Preceding unsigned comment added by Elisky89 (talk • contribs) 21:07, 11 April 2012 (UTC)[reply]

Scaffold speculations

Being on the field of MAPK research for several years now, I am still surprised how easily people are swayed by popular, yet faulty theories, such as "scaffolds". In the recent years, research has made a lot of facts much clearer. Thus there are no more "big protein blobs capable of mediating anything you wish". With the advent of structural biology, we know more about what is possible and what is not. It is also becoming inceasingly clear that most MAPK scaffolds (with the exception of Ste5) actually do not assemble functional ternary complexes, let alone quaternary ones! In accordance with these results, it is actually not possible to demonstrate that JIPs facilitate signaling on-scaffold (see the articles cited). I dare those who think otherwise to try that out in their labs! - Bubus (talk) 22:43, 29 December 2012 (UTC)[reply]