Sandbox 179
From Proteopedia
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{{STRUCTURE_5pep| PDB=5pep | SCENE=Sandbox_179/Scenedefault/2}} | {{STRUCTURE_5pep| PDB=5pep | SCENE=Sandbox_179/Scenedefault/2}} | ||
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Protein Function | Protein Function | ||
Revision as of 04:50, 24 March 2010
| Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. Andrea Gorrell. | |||||||||
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| 5pep, resolution 2.34Å () | |||||||||
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| Activity: | Pepsin A, with EC number 3.4.23.1 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Protein Function
Pepsin is one of three proteolytic, or protein degrading enzymes in the digestive system. It resides in the alimentary canal and is produced by mucosal cells. Pepsin degrades peptides, and is optimally active at low pHs [1]. Pepsin is an aspartic proteinase, more specifically a eukaryotic aspartic protease enzyme. Pepsin was among the first enzymes to be isolated in crystalline form [2]. Aspartic proteinases are widespread in nature, and pepsin in particular has been known to be medically important [3].
Overall Structure
References
- ↑ Cooper JB, Khan G, Taylor G, Tickle IJ, Blundell TL. X-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3 A resolution. J Mol Biol. 1990 Jul 5;214(1):199-222. PMID:2115088
- ↑ Abad-Zapatero C, Rydel TJ, Erickson J. Revised 2.3 A structure of porcine pepsin: evidence for a flexible subdomain. Proteins. 1990;8(1):62-81. PMID:2217165 doi:http://dx.doi.org/10.1002/prot.340080109
- ↑ The prosegment catalyzed pepsin folding to a kinetically trapped native state. Biochemistry 49:365-371
