Sandbox Reserved 938: Difference between revisions

Line 17:

===N-terminal domain===

Here is the <scene name='57/579708/N_zoom_rainbow/2'>N-terminal domain</scene> of the protein.

Here is the <scene name='57/579708/N_zoom_rainbow/2'>N-terminal domain</scene> of the protein. MANF N-terminus is a saposin-like domain (SAPLIP). SAPLIPs, although they have a rather low sequence homology, have a high structural homology and seem to all share the ability to binf lipids [Reference]. However, since the biological receptor and interaction partners are either completely (receptor(s)) or largely (interactions with other proteins) unknown, the precise molecular mechanisms remain elusive. However, it has been proposed, that the neuroprotective ability of MANF may reside in it's N-terminal domain.

===C-terminal domain===

Here is the <scene name='57/579708/C_zoom_rainbow/2'>C-terminal domain</scene> of the protein.

Here is the <scene name='57/579708/C_zoom_rainbow/2'>C-terminal domain</scene> of the protein. It is worth mentioning that residues 138-158 are not visible in the crystal structure, probably due to being natively unstructured. This also includes a RTDL sequence, which is homologous to the KDEL sequence, an ER-retention sequence. This places MANF biologically into the endoplasmic reticulum and the CKGC disulphide bridge, present also in the same region of the protein, suggests a role in ER-stress response. The same type of CKGC disulphide bridge is namely present in the reductases and disulphide isomerases. Thus, it has been suggested, that ER-stress response function may reside in the C-terminus of the protein.

==MANF in disease==

Sandbox Reserved 938: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 17: / Line 17: @@
 ===N-terminal domain===
-Here is the <scene name='57/579708/N_zoom_rainbow/2'>N-terminal domain</scene> of the protein.
+Here is the <scene name='57/579708/N_zoom_rainbow/2'>N-terminal domain</scene> of the protein. MANF N-terminus is a saposin-like domain (SAPLIP). SAPLIPs, although they have a rather low sequence homology, have a high structural homology and seem to all share the ability to binf lipids [Reference]. However, since the biological receptor and interaction partners are either completely (receptor(s)) or largely (interactions with other proteins) unknown, the precise molecular mechanisms remain elusive. However, it has been proposed, that the neuroprotective ability of MANF may reside in it's N-terminal domain.
 ===C-terminal domain===
-Here is the <scene name='57/579708/C_zoom_rainbow/2'>C-terminal domain</scene> of the protein.
+Here is the <scene name='57/579708/C_zoom_rainbow/2'>C-terminal domain</scene> of the protein. It is worth mentioning that residues 138-158 are not visible in the crystal structure, probably due to being natively unstructured. This also includes a RTDL sequence, which is homologous to the KDEL sequence, an ER-retention sequence. This places MANF biologically into the endoplasmic reticulum and the CKGC disulphide bridge, present also in the same region of the protein, suggests a role in ER-stress response. The same type of CKGC disulphide bridge is namely present in the reductases and disulphide isomerases. Thus, it has been suggested, that ER-stress response function may reside in the C-terminus of the protein.
 ==MANF in disease==