Sandbox Reserved 938
From Proteopedia
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==Introduction== | ==Introduction== | ||
| - | Mesencephalic | + | Mesencephalic Astrocyte-derived Neurotrophic Factor (MANF) forms an evultionarily conserved distinct family of growth factors together with the Cerebral Dopamine Neurotrophic Factor (CDNF) [Reference]. MANF was first discovered as an arginine rich protein, which was mutated in early stage tumors, thus it's earlier name ARMET-1 (Arginine-Rich, Mutated in Early-stage Tumors). Since it's discovery, it has been widely studied and has proven useful in a number of experimental setups, among which protective functions in models of strok [Reference], 6-hydroxy dopamine [Reference]. It's receptor remains still to be discovered, however lately a rather intruiging finding was published, namely the interaction between MANF and glucose related protein 78 (GRP78), a protein of the unfolded protein response (UPR) [Reference]. This suggests another important role for MANF in the regulation of UPR, a ubiquitously occuring process in a living organism and evolutionarily heavily conserved. |
| - | + | In (year?) the crystal structure of MANF was solved by Parkash et al, giving important insight into the function of MANF. The further content of this page is directed to dissecting the structure/function relation of the MANF protein. | |
| - | + | <StructureSection load='2W51' size='350' side='right' caption='MANF' scene='57/579708/Manf_rainbow/2'> | |
==The structure of MANF== | ==The structure of MANF== | ||
| - | MANF has 2 distinc and also functionally different domains, C-terminal and N-terminal, connected by | + | MANF has 2 distinc and also functionally different domains, C-terminal and N-terminal, connected by an unstructured loop. There are 4 S-S bridges formed in the molecule, 3 of which in the N-terminal and 1 in the C-terminal domain. The structure suggests and other experiments [Reference] confirm (at least) a dual function of the protein, since the two domains of which it consists, are rather different from one another and show structural similarity to functionally very distinct proteins. |
==N-terminal domain== | ==N-terminal domain== | ||
Revision as of 11:08, 9 May 2014
| This Sandbox is Reserved from 01/04/2014, through 30/06/2014 for use in the course "510042. Protein structure, function and folding" taught by Prof Adrian Goldman, Tommi Kajander, Taru Meri, Konstantin Kogan and Juho Kellosalo at the University of Helsinki. This reservation includes Sandbox Reserved 923 through Sandbox Reserved 947. |
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Introduction
Mesencephalic Astrocyte-derived Neurotrophic Factor (MANF) forms an evultionarily conserved distinct family of growth factors together with the Cerebral Dopamine Neurotrophic Factor (CDNF) [Reference]. MANF was first discovered as an arginine rich protein, which was mutated in early stage tumors, thus it's earlier name ARMET-1 (Arginine-Rich, Mutated in Early-stage Tumors). Since it's discovery, it has been widely studied and has proven useful in a number of experimental setups, among which protective functions in models of strok [Reference], 6-hydroxy dopamine [Reference]. It's receptor remains still to be discovered, however lately a rather intruiging finding was published, namely the interaction between MANF and glucose related protein 78 (GRP78), a protein of the unfolded protein response (UPR) [Reference]. This suggests another important role for MANF in the regulation of UPR, a ubiquitously occuring process in a living organism and evolutionarily heavily conserved.
In (year?) the crystal structure of MANF was solved by Parkash et al, giving important insight into the function of MANF. The further content of this page is directed to dissecting the structure/function relation of the MANF protein.
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