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 2.36&Aring;" /> '''ACTIVATION INTERMED...)
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[[Image:1avf.gif|left|200px]]<br />
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[[Image:1avf.gif|left|200px]]<br /><applet load="1avf" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1avf" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1avf, resolution 2.36&Aring;" />
caption="1avf, resolution 2.36&Aring;" />
'''ACTIVATION INTERMEDIATE 2 OF HUMAN GASTRICSIN FROM HUMAN STOMACH'''<br />
'''ACTIVATION INTERMEDIATE 2 OF HUMAN GASTRICSIN FROM HUMAN STOMACH'''<br />
==Overview==
==Overview==
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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.
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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==
==Disease==
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==About this Structure==
==About this Structure==
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1AVF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AVF OCA].
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1AVF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AVF OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Cherney, M.M.]]
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[[Category: Cherney, M M.]]
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[[Category: James, M.N.G.]]
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[[Category: James, M N.G.]]
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[[Category: Khan, A.R.]]
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[[Category: Khan, A R.]]
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[[Category: Tarasova, N.I.]]
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[[Category: Tarasova, N I.]]
[[Category: NA]]
[[Category: NA]]
[[Category: acid]]
[[Category: acid]]
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[[Category: intermediate]]
[[Category: intermediate]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:02:30 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:39 2008''

Revision as of 09:48, 21 February 2008


1avf, resolution 2.36Å

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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 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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