Sandbox Reserved 938

From Proteopedia

proteopedia linkproteopedia link

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.

To get started: Click the edit this page tab at the top. Save the page after each step, then edit it again. Click the 3D button (when editing, above the wikitext box) to insert Jmol. show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page. Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc. More help: Help:Editing

Introduction

Mesencephalic astrocyte-derived neurotrophic factor (MANF), protein family, discovery as a protein, biological function (toxin studies, stroke, etc. - Mikko, ER-stress - Apostolou, Glembotski, etc). Receptor unknown despite broad array of function. Knock-out has been recently published, giving more broader insight into the structure-function relationship of the protein.

spinqualitylabelsall models MANF Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Everything here Contents 1 The structure of MANF 2 N-terminal domain 3 C-terminal domain 4 MANF in disease The structure of MANF MANF has 2 distinc and also functionally different domains, C-terminal and N-terminal, connected by a loop. SS-bridges? ER-retention-signal significance and more precise structure-function discussion. N-terminal domain Here is the of the protein. C-terminal domain Here is the of the protein. MANF in disease

References