2i9s is a 1 chain structure with sequence from Mus musculus. Full experimental 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
Mesoderm development (MESD) is a 224 amino acid mouse protein that acts as a molecular chaperone for receptors of the low-density lipoprotein receptor (LDLR) family. By recording (15)N-HSQC-NMR spectra of six different MESD constructs, we could determine a highly structured core region corresponding to residues 104-177. Here we firstly present the solution structure of this highly conserved core of MESD. It shows a four-stranded anti-parallel beta-sheet and two alpha-helices situated on one side of the sheet. Although described in the literature as structurally homologues to ferredoxins, the connectivity of secondary structure elements is different in the MESD fold. A structural comparison to entries of the PDB reveals a frequent domain with low sequence homology annotated as HMA and P-II domains in Pfam.
The solution structure of the core of mesoderm development (MESD), a chaperone for members of the LDLR-family.,Kohler C, Andersen OM, Diehl A, Krause G, Schmieder P, Oschkinat H J Struct Funct Genomics. 2006 Dec;7(3-4):131-8. Epub 2007 Mar 7. PMID:17342452[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Kohler C, Andersen OM, Diehl A, Krause G, Schmieder P, Oschkinat H. The solution structure of the core of mesoderm development (MESD), a chaperone for members of the LDLR-family. J Struct Funct Genomics. 2006 Dec;7(3-4):131-8. Epub 2007 Mar 7. PMID:17342452 doi:10.1007/s10969-007-9016-5
