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	== Structure ==		== Structure ==
-		+	The structure of AGR2 consists of an unstructured N-terminal with a thioredoxin fold, intermolecular salt bridges and is a monomer dimer [3]. The unstructured N-terminal with the thioredoxin fold accounts for cell adhesion and the thioredoxin protein is associated with redox signaling to reduce other proteins and electron transfer signaling [3]. The intermolecular salt bridges account for stabilization and it is a monomer dimer because of its single chain structure [3].
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	== Function ==		== Function ==

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Revision as of 19:20, 26 April 2013

This Sandbox is Reserved from Feb 1, 2013, through May 10, 2013 for use in the course "Biochemistry" taught by Irma Santoro at the Reinhardt University. This reservation includes Sandbox Reserved 591 through Sandbox Reserved 599.

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

I would like the page to have a table of contents and the following main sections: Background, Structure (with a jmol image area), Function, Clinical Relevance, and References.

Contents 1 Background 2 Structure 3 Function 4 Clinical Relevance 5 References

Background

Anterior gradient protein 2 is also known as Gob-4, hAG-2 and in Xenopus laevis, the African clawed toad, XAG-2 [6]. It is not only a secretory protein, it is also an endoplasmic reticulum protein responsible for the progression of metastatic cancers in humans, and in Xenopus laevis, tissue development [6]. It was first discovered in Xenopus laevis in the mucus secreting cement gland which allows for organogenesis of this organism [5]. Organogenesis is when the ectoderm, endoderm, and mesoderm develop in an organism's internal organs and other tissue differentiation such as: limb regeneration, forebrain formation and cellular differentiation and development [5]. In humans, AGR2 was discovered in a breast cancer study in which the AGR2 gene was cloned and immunohistochemical staining was used to determine its presence in the carcinoma cell lines of the cancer patients [7].

Structure

The structure of AGR2 consists of an unstructured N-terminal with a thioredoxin fold, intermolecular salt bridges and is a monomer dimer [3]. The unstructured N-terminal with the thioredoxin fold accounts for cell adhesion and the thioredoxin protein is associated with redox signaling to reduce other proteins and electron transfer signaling [3]. The intermolecular salt bridges account for stabilization and it is a monomer dimer because of its single chain structure [3].

Function

Clinical Relevance

References

spinqualitylabelsall models Anterior Gradient Protein 2 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image