1gvl
From Proteopedia
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| - | [[Image:1gvl.jpg|left|200px]] | + | [[Image:1gvl.jpg|left|200px]] |
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| - | '''HUMAN PROKALLIKREIN 6 (HK6)/ PROZYME/ PROPROTEASE M/ PRONEUROSIN''' | + | {{Structure |
| + | |PDB= 1gvl |SIZE=350|CAPTION= <scene name='initialview01'>1gvl</scene>, resolution 1.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''HUMAN PROKALLIKREIN 6 (HK6)/ PROZYME/ PROPROTEASE M/ PRONEUROSIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GVL is a [ | + | 1GVL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GVL OCA]. |
==Reference== | ==Reference== | ||
| - | The structure of human prokallikrein 6 reveals a novel activation mechanism for the kallikrein family., Gomis-Ruth FX, Bayes A, Sotiropoulou G, Pampalakis G, Tsetsenis T, Villegas V, Aviles FX, Coll M, J Biol Chem. 2002 Jul 26;277(30):27273-81. Epub 2002 May 16. PMID:[http:// | + | The structure of human prokallikrein 6 reveals a novel activation mechanism for the kallikrein family., Gomis-Ruth FX, Bayes A, Sotiropoulou G, Pampalakis G, Tsetsenis T, Villegas V, Aviles FX, Coll M, J Biol Chem. 2002 Jul 26;277(30):27273-81. Epub 2002 May 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12016211 12016211] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zymogen]] | [[Category: zymogen]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:28:32 2008'' |
Revision as of 09:28, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN PROKALLIKREIN 6 (HK6)/ PROZYME/ PROPROTEASE M/ PRONEUROSIN
Overview
Zyme/protease M/neurosin/human kallikrein 6 (hK6) is a member of the human kallikrein family of trypsin-like serine proteinases and was originally identified as being down-regulated in metastatic breast and ovarian tumors when compared with corresponding primary tumors. Recent evidence suggests that hK6 may serve as a circulating tumor marker in ovarian cancers. In addition, it was described in the brain of Parkinson's disease and Alzheimer's disease patients, where it is implicated in amyloid precursor protein processing. It is thus a biomarker for these diseases. To examine the mechanism of activation of hK6, we have solved the structure of its proform, the first of a human kallikrein family member. The proenzyme displays a fold that exhibits chimeric features between those of trypsinogen and other family members. It lacks the characteristic "kallikrein loop" and forms the six disulfide bridges of trypsin. Pro-hK6 displays a completely closed specificity pocket and a unique conformation of the regions involved in structural rearrangements upon proteolytic cleavage activation. This points to a novel activation mechanism, which could be extrapolated to other human kallikreins.
About this Structure
1GVL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The structure of human prokallikrein 6 reveals a novel activation mechanism for the kallikrein family., Gomis-Ruth FX, Bayes A, Sotiropoulou G, Pampalakis G, Tsetsenis T, Villegas V, Aviles FX, Coll M, J Biol Chem. 2002 Jul 26;277(30):27273-81. Epub 2002 May 16. PMID:12016211
Page seeded by OCA on Thu Mar 20 11:28:32 2008
