1AVF
ACTIVATION INTERMEDIATE 2 OF HUMAN GASTRICSIN FROM HUMAN STOMACH
Summary for 1AVF
| Entry DOI | 10.2210/pdb1avf/pdb |
| Descriptor | GASTRICSIN, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | aspartyl protease, gastricsin, aspartic proteinase, intermediate, activation, acid |
| Biological source | Homo sapiens (human) More |
| Cellular location | Secreted: P20142 P20142 |
| Total number of polymer chains | 4 |
| Total formula weight | 76920.20 |
| Authors | Khan, A.R.,Cherney, M.M.,Tarasova, N.I.,James, M.N.G. (deposition date: 1997-09-16, release date: 1998-02-25, Last modification date: 2024-10-30) |
| Primary citation | Khan, A.R.,Cherney, M.M.,Tarasova, N.I.,James, M.N. Structural characterization of activation 'intermediate 2' on the pathway to human gastricsin. Nat.Struct.Biol., 4:1010-1015, 1997 Cited by PubMed Abstract: 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. PubMed: 9406551DOI: 10.1038/nsb1297-1010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.36 Å) |
Structure validation
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