1ijl

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(New page: 200px<br /><applet load="1ijl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ijl, resolution 2.6&Aring;" /> '''Crystal structure of ...)
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[[Image:1ijl.jpg|left|200px]]<br /><applet load="1ijl" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ijl.jpg|left|200px]]<br /><applet load="1ijl" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ijl, resolution 2.6&Aring;" />
caption="1ijl, resolution 2.6&Aring;" />
'''Crystal structure of acidic phospholipase A2 from deinagkistrodon acutus'''<br />
'''Crystal structure of acidic phospholipase A2 from deinagkistrodon acutus'''<br />
==Overview==
==Overview==
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An acidic phospholipase A(2) was purified from Deinagkistrodon acutus, (Agkistrodon acutus) which displays an inhibitory effect on platelet, aggregation. The three-dimensional structure of the enzyme was determined, by molecular replacement at 2.6 A resolution with a crystallographic R, factor of 18.40% (R(free) = 22.50%) and reasonable stereochemistry. Two, molecules in the asymmetric unit form a dimer and the dimer formation, accompanies a significant conformational adaptation of segment 14-23, a, constituent of the 'interface recognition site' (IRS). This probably, reflects the inherent structural flexibility of the IRS. The possible, expansion of the site for inhibiting platelet aggregation as proposed, previously [Wang et al. (1996), J. Mol. Biol. 255, 669-676] is discussed.
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An acidic phospholipase A(2) was purified from Deinagkistrodon acutus (Agkistrodon acutus) which displays an inhibitory effect on platelet aggregation. The three-dimensional structure of the enzyme was determined by molecular replacement at 2.6 A resolution with a crystallographic R factor of 18.40% (R(free) = 22.50%) and reasonable stereochemistry. Two molecules in the asymmetric unit form a dimer and the dimer formation accompanies a significant conformational adaptation of segment 14-23, a constituent of the 'interface recognition site' (IRS). This probably reflects the inherent structural flexibility of the IRS. The possible expansion of the site for inhibiting platelet aggregation as proposed previously [Wang et al. (1996), J. Mol. Biol. 255, 669-676] is discussed.
==About this Structure==
==About this Structure==
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1IJL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinagkistrodon_acutus Deinagkistrodon acutus] with ZN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IJL OCA].
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1IJL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinagkistrodon_acutus Deinagkistrodon acutus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IJL OCA].
==Reference==
==Reference==
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[[Category: three long helix]]
[[Category: three long helix]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:27:19 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:12:38 2008''

Revision as of 11:12, 21 February 2008


1ijl, resolution 2.6Å

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Crystal structure of acidic phospholipase A2 from deinagkistrodon acutus

Overview

An acidic phospholipase A(2) was purified from Deinagkistrodon acutus (Agkistrodon acutus) which displays an inhibitory effect on platelet aggregation. The three-dimensional structure of the enzyme was determined by molecular replacement at 2.6 A resolution with a crystallographic R factor of 18.40% (R(free) = 22.50%) and reasonable stereochemistry. Two molecules in the asymmetric unit form a dimer and the dimer formation accompanies a significant conformational adaptation of segment 14-23, a constituent of the 'interface recognition site' (IRS). This probably reflects the inherent structural flexibility of the IRS. The possible expansion of the site for inhibiting platelet aggregation as proposed previously [Wang et al. (1996), J. Mol. Biol. 255, 669-676] is discussed.

About this Structure

1IJL is a Single protein structure of sequence from Deinagkistrodon acutus with and as ligands. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.

Reference

Structure of an acidic phospholipase A2 from the venom of Deinagkistrodon acutus., Gu L, Zhang H, Song S, Zhou Y, Lin Z, Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):104-10. Epub 2001, Dec 21. PMID:11752784

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