1cvi
From Proteopedia
(New page: 200px<br /> <applet load="1cvi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cvi, resolution 3.20Å" /> '''CRYSTAL STRUCTURE O...) |
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| - | [[Image:1cvi.gif|left|200px]]<br /> | + | [[Image:1cvi.gif|left|200px]]<br /><applet load="1cvi" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1cvi" size=" | + | |
caption="1cvi, resolution 3.20Å" /> | caption="1cvi, resolution 3.20Å" /> | ||
'''CRYSTAL STRUCTURE OF HUMAN PROSTATIC ACID PHOSPHATASE'''<br /> | '''CRYSTAL STRUCTURE OF HUMAN PROSTATIC ACID PHOSPHATASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: Prostatic acid phosphatase (hPAP) is a major product of the | + | 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== | ==About this Structure== | ||
| - | 1CVI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG and GLY as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1CVI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=GLY:'>GLY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CVI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Jakob, C | + | [[Category: Jakob, C G.]] |
[[Category: Kuciel, R.]] | [[Category: Kuciel, R.]] | ||
[[Category: Lebioda, L.]] | [[Category: Lebioda, L.]] | ||
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[[Category: inhibition]] | [[Category: inhibition]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:10:10 2008'' |
Revision as of 10:10, 21 February 2008
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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 with and as ligands. Active as Acid phosphatase, with EC number 3.1.3.2 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 Thu Feb 21 12:10:10 2008
Categories: Acid phosphatase | Homo sapiens | Single protein | Jakob, C G. | Kuciel, R. | Lebioda, L. | Lewinski, K. | Ostrowski, W. | GLY | NAG | Inhibition
