1avf: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|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> | |||
}} | }} | ||
| Line 14: | Line 17: | ||
==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. | ||
==About this Structure== | ==About this Structure== | ||
| Line 30: | Line 30: | ||
[[Category: Khan, A R.]] | [[Category: Khan, A R.]] | ||
[[Category: Tarasova, N I.]] | [[Category: Tarasova, N I.]] | ||
[[Category: acid]] | [[Category: acid]] | ||
[[Category: activation]] | [[Category: activation]] | ||
| Line 38: | Line 37: | ||
[[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'' | ||