1lq8

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(New page: 200px<br /> <applet load="1lq8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lq8, resolution 2.40&Aring;" /> '''Crystal structure o...)
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[[Image:1lq8.gif|left|200px]]<br />
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[[Image:1lq8.gif|left|200px]]<br /><applet load="1lq8" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1lq8" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1lq8, resolution 2.40&Aring;" />
caption="1lq8, resolution 2.40&Aring;" />
'''Crystal structure of cleaved protein C inhibitor'''<br />
'''Crystal structure of cleaved protein C inhibitor'''<br />
==Overview==
==Overview==
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Protein C inhibitor (PCI) is a member of the serpin family that has many, biological functions. In blood it acts as a procoagulant, and, in the, seminal vesicles, it is required for spermatogenesis. The activity of PCI, is affected by heparin binding in a manner unique among the heparin, binding serpins, and, in addition, PCI binds hydrophobic hormones with, apparent specificity for retinoids. Here we present the 2.4 A, crystallographic structure of reactive center loop (RCL) cleaved PCI. A, striking feature of the structure is a two-turn N-terminal shortening of, helix A, which creates a large hydrophobic pocket that docking studies, indicate to be the retinoid binding site. On the basis of surface, electrostatic properties, a novel mechanism for heparin activation is, proposed.
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Protein C inhibitor (PCI) is a member of the serpin family that has many biological functions. In blood it acts as a procoagulant, and, in the seminal vesicles, it is required for spermatogenesis. The activity of PCI is affected by heparin binding in a manner unique among the heparin binding serpins, and, in addition, PCI binds hydrophobic hormones with apparent specificity for retinoids. Here we present the 2.4 A crystallographic structure of reactive center loop (RCL) cleaved PCI. A striking feature of the structure is a two-turn N-terminal shortening of helix A, which creates a large hydrophobic pocket that docking studies indicate to be the retinoid binding site. On the basis of surface electrostatic properties, a novel mechanism for heparin activation is proposed.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1LQ8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NDG and IPA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LQ8 OCA].
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1LQ8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NDG:'>NDG</scene> and <scene name='pdbligand=IPA:'>IPA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQ8 OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Huntington, J.A.]]
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[[Category: Huntington, J A.]]
[[Category: Kjellberg, M.]]
[[Category: Kjellberg, M.]]
[[Category: Stenflo, J.]]
[[Category: Stenflo, J.]]
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[[Category: serpin]]
[[Category: serpin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:03:29 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:19 2008''

Revision as of 11:47, 21 February 2008

Image:1lq8.gif

1lq8, resolution 2.40Å

Drag the structure with the mouse to rotate

Crystal structure of cleaved protein C inhibitor

Contents

Overview

Protein C inhibitor (PCI) is a member of the serpin family that has many biological functions. In blood it acts as a procoagulant, and, in the seminal vesicles, it is required for spermatogenesis. The activity of PCI is affected by heparin binding in a manner unique among the heparin binding serpins, and, in addition, PCI binds hydrophobic hormones with apparent specificity for retinoids. Here we present the 2.4 A crystallographic structure of reactive center loop (RCL) cleaved PCI. A striking feature of the structure is a two-turn N-terminal shortening of helix A, which creates a large hydrophobic pocket that docking studies indicate to be the retinoid binding site. On the basis of surface electrostatic properties, a novel mechanism for heparin activation is proposed.

Disease

Known diseases associated with this structure: Protein C inhibitor deficiency OMIM:[601841]

About this Structure

1LQ8 is a Protein complex structure of sequences from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of protein C inhibitor provides insights into hormone binding and heparin activation., Huntington JA, Kjellberg M, Stenflo J, Structure. 2003 Feb;11(2):205-15. PMID:12575940

Page seeded by OCA on Thu Feb 21 13:47:19 2008

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