1xww

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(New page: 200px<br /> <applet load="1xww" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xww, resolution 1.63&Aring;" /> '''Crystal Structure o...)
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'''Crystal Structure of Human B-form Low Molecular Weight Phosphotyrosyl Phosphatase at 1.6 Angstrom Resolution'''<br />
'''Crystal Structure of Human B-form Low Molecular Weight Phosphotyrosyl Phosphatase at 1.6 Angstrom Resolution'''<br />
==Overview==
==Overview==
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The crystal structure of HPTP-B, a human isoenzyme of the low molecular, weight phosphotyrosyl phosphatase (LMW PTPase) is reported here at a, resolution of 1.6 A. This high resolution structure of the second human, LMW PTPase isoenzyme provides the opportunity to examine the structural, basis of different substrate and inhibitor/activator responses. The, crystal packing of HPTP-B positions a normally surface-exposed arginine in, a position equivalent to the tyrosyl substrate. A comparison of all, deposited crystallographic coordinates of these PTPases reveals three, atomic positions within the active site cavity occupied by hydrogen bond, donor or acceptor atoms on bound molecules, suggesting useful design, elements for synthetic inhibitors. A selection of inhibitor and activator, molecules as well as small molecule and peptide substrates were tested, against each human isoenzyme. These results along with the crystal packing, seen in HPTP-B suggest relevant sequence elements in the currently unknown, target sequence.
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The crystal structure of HPTP-B, a human isoenzyme of the low molecular weight phosphotyrosyl phosphatase (LMW PTPase) is reported here at a resolution of 1.6 A. This high resolution structure of the second human LMW PTPase isoenzyme provides the opportunity to examine the structural basis of different substrate and inhibitor/activator responses. The crystal packing of HPTP-B positions a normally surface-exposed arginine in a position equivalent to the tyrosyl substrate. A comparison of all deposited crystallographic coordinates of these PTPases reveals three atomic positions within the active site cavity occupied by hydrogen bond donor or acceptor atoms on bound molecules, suggesting useful design elements for synthetic inhibitors. A selection of inhibitor and activator molecules as well as small molecule and peptide substrates were tested against each human isoenzyme. These results along with the crystal packing seen in HPTP-B suggest relevant sequence elements in the currently unknown target sequence.
==About this Structure==
==About this Structure==
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1XWW 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 SO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XWW OCA].
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1XWW 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=SO4:'>SO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XWW OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Stauffacher, C.V.]]
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[[Category: Stauffacher, C V.]]
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[[Category: Zabell, A.P.R.]]
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[[Category: Zabell, A P.R.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:12:07 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:59:27 2008''

Revision as of 13:59, 21 February 2008


1xww, resolution 1.63Å

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Crystal Structure of Human B-form Low Molecular Weight Phosphotyrosyl Phosphatase at 1.6 Angstrom Resolution

Overview

The crystal structure of HPTP-B, a human isoenzyme of the low molecular weight phosphotyrosyl phosphatase (LMW PTPase) is reported here at a resolution of 1.6 A. This high resolution structure of the second human LMW PTPase isoenzyme provides the opportunity to examine the structural basis of different substrate and inhibitor/activator responses. The crystal packing of HPTP-B positions a normally surface-exposed arginine in a position equivalent to the tyrosyl substrate. A comparison of all deposited crystallographic coordinates of these PTPases reveals three atomic positions within the active site cavity occupied by hydrogen bond donor or acceptor atoms on bound molecules, suggesting useful design elements for synthetic inhibitors. A selection of inhibitor and activator molecules as well as small molecule and peptide substrates were tested against each human isoenzyme. These results along with the crystal packing seen in HPTP-B suggest relevant sequence elements in the currently unknown target sequence.

About this Structure

1XWW is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the human B-form low molecular weight phosphotyrosyl phosphatase at 1.6-A resolution., Zabell AP, Schroff AD Jr, Bain BE, Van Etten RL, Wiest O, Stauffacher CV, J Biol Chem. 2006 Mar 10;281(10):6520-7. Epub 2005 Oct 27. PMID:16253994

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