1avf
From Proteopedia
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|PDB= 1avf |SIZE=350|CAPTION= <scene name='initialview01'>1avf</scene>, resolution 2.36Å | |PDB= 1avf |SIZE=350|CAPTION= <scene name='initialview01'>1avf</scene>, resolution 2.36Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene> | + | |LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Gastricsin Gastricsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.3 3.4.23.3] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Gastricsin Gastricsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.3 3.4.23.3] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1avf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1avf OCA], [http://www.ebi.ac.uk/pdbsum/1avf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1avf RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=608886 608886]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Khan, A R.]] | [[Category: Khan, A R.]] | ||
[[Category: Tarasova, N I.]] | [[Category: Tarasova, N I.]] | ||
| - | [[Category: NA]] | ||
[[Category: acid]] | [[Category: acid]] | ||
[[Category: activation]] | [[Category: activation]] | ||
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[[Category: intermediate]] | [[Category: intermediate]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:48:17 2008'' |
Revision as of 15:48, 30 March 2008
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| , resolution 2.36Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Gastricsin, with EC number 3.4.23.3 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ACTIVATION INTERMEDIATE 2 OF HUMAN GASTRICSIN FROM HUMAN STOMACH
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.
About this Structure
1AVF is a Protein complex structure of sequences from Homo sapiens. 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
Page seeded by OCA on Sun Mar 30 18:48:17 2008
