1lq8
From Proteopedia
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|PDB= 1lq8 |SIZE=350|CAPTION= <scene name='initialview01'>1lq8</scene>, resolution 2.40Å | |PDB= 1lq8 |SIZE=350|CAPTION= <scene name='initialview01'>1lq8</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</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> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ezx|1EZX]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lq8 OCA], [http://www.ebi.ac.uk/pdbsum/1lq8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lq8 RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601841 601841]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Kjellberg, M.]] | [[Category: Kjellberg, M.]] | ||
[[Category: Stenflo, J.]] | [[Category: Stenflo, J.]] | ||
| - | [[Category: IPA]] | ||
| - | [[Category: NDG]] | ||
[[Category: heparin]] | [[Category: heparin]] | ||
[[Category: inhibitor]] | [[Category: inhibitor]] | ||
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[[Category: serpin]] | [[Category: serpin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:05:58 2008'' |
Revision as of 19:05, 30 March 2008
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| , resolution 2.40Å | |||||||
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| Ligands: | , , , | ||||||
| Related: | 1EZX
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of cleaved protein C inhibitor
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.
About this Structure
1LQ8 is a Protein complex structure of sequences from Homo sapiens. 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 Sun Mar 30 22:05:58 2008
