1avf | pdb_00001avf

ACTIVATION INTERMEDIATE 2 OF HUMAN GASTRICSIN FROM HUMAN STOMACH

spinqualitylabelsall models 1avf, resolution 2.36Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1avf is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NA Activity: Gastricsin, with EC number 3.4.23.3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PEPC_HUMAN] Hydrolyzes a variety of proteins. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The crystal structure of an activation intermediate of human gastricsin has been determined at 2.4 A resolution. The human digestive enzyme gastricsin (pepsin C) is an aspartic proteinase that is synthesized as the inactive precursor (zymogen) progastricsin (pepsinogen C or hPGC). In the zymogen, a positively-charged N-terminal prosegment of 43 residues (Ala 1p-Leu 43p; the suffix 'p' refers to the prosegment) sterically prevents the approach of a substrate to the active site. Zymogen conversion occurs in an autocatalytic and stepwise fashion at low pH through the formation of intermediates. The structure of the non-covalent complex of a partially-cleaved peptide of the prosegment (Ala 1p-Phe 26p) with mature gastricsin (Ser 1-Ala 329) suggests an activation pathway that may be common to all gastric aspartic proteinases. Structural characterization of activation 'intermediate 2' on the pathway to human gastricsin.,Khan AR, Cherney MM, Tarasova NI, James MN Nat Struct Biol. 1997 Dec;4(12):1010-5. PMID:9406551 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pepsin

Proteopedia Page Contributors and Editors (what is this?)

OCA