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.
2i9s
From Proteopedia
|
The solution structure of the core of mesoderm development (MESD).
Overview
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.
About this Structure
2I9S is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
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. 2007 Mar 7;. PMID:17342452
Page seeded by OCA on Wed Nov 21 12:12:02 2007
