Köhler Christian, Andersen Olav M, Diehl Annette, Krause Gerd, Schmieder Peter, Oschkinat Hartmut
Department of NMR-Supported Structural Biology, Leibniz-Institut für Molekulare Pharmakologie, Robert-Rössle-Str. 10, 13125 Berlin, Germany.
J Struct Funct Genomics. 2006 Dec;7(3-4):131-8. doi: 10.1007/s10969-007-9016-5. Epub 2007 Mar 7.
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.
中胚层发育蛋白（MESD）是一种由224个氨基酸组成的小鼠蛋白，它作为低密度脂蛋白受体（LDLR）家族受体的分子伴侣发挥作用。通过记录六种不同MESD构建体的（15）N-HSQC-NMR谱，我们能够确定对应于残基104 - 177的高度结构化核心区域。在此，我们首先展示MESD这个高度保守核心的溶液结构。它呈现出一个四链反平行β折叠片和位于该片一侧的两个α螺旋。尽管在文献中被描述为与铁氧化还原蛋白结构同源，但在MESD折叠中二级结构元件的连接方式不同。与蛋白质数据银行（PDB）条目的结构比较揭示了一个在Pfam中注释为HMA和P-II结构域的低序列同源性的常见结构域。
