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2hpa

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[[Image:2hpa.gif|left|200px]]
[[Image:2hpa.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2hpa |SIZE=350|CAPTION= <scene name='initialview01'>2hpa</scene>, resolution 2.90&Aring;
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The line below this paragraph, containing "STRUCTURE_2hpa", 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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=PT3:N-PROPYL-TARTRAMIC+ACID'>PT3</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_2hpa| PDB=2hpa | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hpa OCA], [http://www.ebi.ac.uk/pdbsum/2hpa PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hpa RCSB]</span>
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}}
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'''STRUCTURAL ORIGINS OF L(+)-TARTRATE INHIBITION OF HUMAN PROSTATIC ACID PHOSPHATASE'''
'''STRUCTURAL ORIGINS OF L(+)-TARTRATE INHIBITION OF HUMAN PROSTATIC ACID PHOSPHATASE'''
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[[Category: Lacount, M W.]]
[[Category: Lacount, M W.]]
[[Category: Lebioda, L.]]
[[Category: Lebioda, L.]]
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[[Category: acid phosphatase]]
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[[Category: Acid phosphatase]]
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[[Category: n-propyltartramate]]
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[[Category: N-propyltartramate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:32:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:33:26 2008''
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Revision as of 03:32, 4 May 2008

Template:STRUCTURE 2hpa

STRUCTURAL ORIGINS OF L(+)-TARTRATE INHIBITION OF HUMAN PROSTATIC ACID PHOSPHATASE


Overview

Acid phosphatase activity in the blood serum is usually separated into tartrate-resistant and tartrate-refractory, which is reported as the prostatic acid phosphatase level. Human prostatic acid phosphatase crystals soaked in N-propyl-L-tartramate were used to collect x-ray diffraction data to 2.9 A resolution under cryogenic conditions. Positive difference electron density, corresponding to the inhibitor, was found. The quality of the electron density maps clearly shows the orientation of the carboxylate and N-propyl-substituted amide groups. The hydroxyl group attached to C3 forms two crucial hydrogen bonds with Arg-79 and His-257. Previous crystallographic studies compiled on the tartrate-rat prostatic acid phosphatase binary complex (Lindqvist, Y., Schneider, G., and Vihko, P. (1993) J. Biol. Chem. 268, 20744-20746) erroneously positioned D-tartrate into the active site. Modeling studies have shown that the C3 hydroxyl group on the D(-)-stereoisomer of tartrate, which does not significantly inhibit prostatic acid phosphatase, does not form strong hydrogen bonds with Arg-79 or His-257. The structure of human prostatic acid phosphatase, noncovalently bound in N-propyl-L-tartramate, is used to develop inhibitors with higher specificity and potency than L(+)-tartrate.

About this Structure

2HPA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural origins of L(+)-tartrate inhibition of human prostatic acid phosphatase., LaCount MW, Handy G, Lebioda L, J Biol Chem. 1998 Nov 13;273(46):30406-9. PMID:9804805 Page seeded by OCA on Sun May 4 06:32:38 2008

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