2hpa

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[[Image:2hpa.gif|left|200px]]<br /><applet load="2hpa" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2hpa.gif|left|200px]]
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caption="2hpa, resolution 2.90&Aring;" />
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'''STRUCTURAL ORIGINS OF L(+)-TARTRATE INHIBITION OF HUMAN PROSTATIC ACID PHOSPHATASE'''<br />
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{{Structure
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|PDB= 2hpa |SIZE=350|CAPTION= <scene name='initialview01'>2hpa</scene>, resolution 2.90&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene> and <scene name='pdbligand=PT3:N-PROPYL-TARTRAMIC ACID'>PT3</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''STRUCTURAL ORIGINS OF L(+)-TARTRATE INHIBITION OF HUMAN PROSTATIC ACID PHOSPHATASE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2HPA 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>, <scene name='pdbligand=NDG:'>NDG</scene> and <scene name='pdbligand=PT3:'>PT3</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=2HPA OCA].
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2HPA 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=2HPA OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9804805 9804805]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9804805 9804805]
[[Category: Acid phosphatase]]
[[Category: Acid phosphatase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: n-propyltartramate]]
[[Category: n-propyltartramate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:44:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:19:47 2008''

Revision as of 15:19, 20 March 2008

Image:2hpa.gif


PDB ID 2hpa

Drag the structure with the mouse to rotate
, resolution 2.90Å
Ligands: , and
Activity: Acid phosphatase, with EC number 3.1.3.2
Coordinates: save as pdb, mmCIF, xml



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

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