1cvi

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[[Image:1cvi.gif|left|200px]]
[[Image:1cvi.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1cvi |SIZE=350|CAPTION= <scene name='initialview01'>1cvi</scene>, resolution 3.20&Aring;
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The line below this paragraph, containing "STRUCTURE_1cvi", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1cvi| PDB=1cvi | SCENE= }}
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|RELATEDENTRY=[[2hpa|2HPA]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cvi OCA], [http://www.ebi.ac.uk/pdbsum/1cvi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cvi RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF HUMAN PROSTATIC ACID PHOSPHATASE'''
'''CRYSTAL STRUCTURE OF HUMAN PROSTATIC ACID PHOSPHATASE'''
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[[Category: Lewinski, K.]]
[[Category: Lewinski, K.]]
[[Category: Ostrowski, W.]]
[[Category: Ostrowski, W.]]
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[[Category: acid phosphatase]]
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[[Category: Acid phosphatase]]
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[[Category: inhibition]]
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[[Category: Inhibition]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:09:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:29:18 2008''
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Revision as of 10:09, 2 May 2008

Image:1cvi.gif

Template:STRUCTURE 1cvi

CRYSTAL STRUCTURE OF HUMAN PROSTATIC ACID PHOSPHATASE


Overview

BACKGROUND: Prostatic acid phosphatase (hPAP) is a major product of the human prostate gland, yet its physiological substrate remains unknown. METHODS: Human PAP, purified from semen, was crystallized using polyethylene glycol as the precipitant and its crystal structure was determined using X-ray diffraction. The structure was refined at 3.1 A resolution to R = 16% and R(free) = 27%. RESULTS: The structure of hPAP is similar to that of other known histidine phosphatases, and the positions of its catalytic residues are conserved. N-linked carbohydrates are present at each of the possible glycosylation sites. It appears that high-mannose chains are attached to Asn 62 and Asp 301, while complex chains are at Asn 188. CONCLUSIONS: The similarity of the three-dimensional structures of rat PAP and human PAP indicates that the mechanistic analyses of the catalytic mechanism proposed for the rat enzyme should be extended to the human enzyme without reservations. The crystallographic data allowed the correlation of attachment sites of N-linked carbohydrate chains with a given carbohydrate type. The carbohydrates of the protein produced in the prostate cells and in the baculovirus expression system appear to differ at the site of complex carbohydrates attachment.

About this Structure

1CVI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human prostatic acid phosphatase ., Jakob CG, Lewinski K, Kuciel R, Ostrowski W, Lebioda L, Prostate. 2000 Feb 15;42(3):211-8. PMID:10639192 Page seeded by OCA on Fri May 2 13:09:19 2008

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