1avf
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(New page: 200px<br /> <applet load="1avf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1avf, resolution 2.36Å" /> '''ACTIVATION INTERMED...)
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Revision as of 13:56, 12 November 2007
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ACTIVATION INTERMEDIATE 2 OF HUMAN GASTRICSIN FROM HUMAN STOMACH
Contents |
Overview
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.
Disease
Known disease associated with this structure: Obesity, variation in OMIM:[608886]
About this Structure
1AVF is a Protein complex structure of sequences from Homo sapiens with NA as ligand. Active as Gastricsin, with EC number 3.4.23.3 Full crystallographic information is available from OCA.
Reference
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
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