This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1ig7
From Proteopedia
Revision as of 13:39, 28 September 2014 by OCA (Talk | contribs)
1ig7 is a 3 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The Msx-1 homeodomain protein plays a crucial role in craniofacial, limb, and nervous system development. Homeodomain DNA-binding domains are comprised of 60 amino acids that show a high degree of evolutionary conservation. We have determined the structure of the Msx-1 homeodomain complexed to DNA at 2.2 A resolution. The structure has an unusually well-ordered N-terminal arm with a unique trajectory across the minor groove of the DNA. DNA specificity conferred by bases flanking the core TAAT sequence is explained by well ordered water-mediated interactions at Q50. Most interactions seen at the TAAT sequence are typical of the interactions seen in other homeodomain structures. Comparison of the Msx-1-HD structure to all other high resolution HD-DNA complex structures indicate a remarkably well-conserved sphere of hydration between the DNA and protein in these complexes.
Crystal structure of the Msx-1 homeodomain/DNA complex.,Hovde S, Abate-Shen C, Geiger JH Biochemistry. 2001 Oct 9;40(40):12013-21. PMID:11580277[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Hovde S, Abate-Shen C, Geiger JH. Crystal structure of the Msx-1 homeodomain/DNA complex. Biochemistry. 2001 Oct 9;40(40):12013-21. PMID:11580277
