2i9s: Difference between revisions

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==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.

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==

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==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17342452 17342452]

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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17342452 17342452]

[[Category: Mus musculus]]

[[Category: Single protein]]

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[[Category: ferredoxin-like-fold]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 10: / Line 10: @@
 ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17342452 17342452]
+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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17342452 17342452]
 [[Category: Mus musculus]]
 [[Category: Single protein]]
@@ Line 21: / Line 21: @@
 [[Category: ferredoxin-like-fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:22:52 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:50:23 2008''