1e04
From Proteopedia
(New page: 200px<br /> <applet load="1e04" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e04, resolution 2.6Å" /> '''PLASMA BETA ANTITHRO...) |
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| - | [[Image:1e04.gif|left|200px]]<br /> | + | [[Image:1e04.gif|left|200px]]<br /><applet load="1e04" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1e04" size=" | + | |
caption="1e04, resolution 2.6Å" /> | caption="1e04, resolution 2.6Å" /> | ||
'''PLASMA BETA ANTITHROMBIN-III'''<br /> | '''PLASMA BETA ANTITHROMBIN-III'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of a dimeric form of intact antithrombin has been | + | The crystal structure of a dimeric form of intact antithrombin has been solved to 2.6 A, representing the highest-resolution structure of an active, inhibitory serpin to date. The crystals were grown under microgravity conditions on Space Shuttle mission STS-67. The overall confidence in the structure, determined earlier from lower resolution data, is increased and new insights into the structure-function relationship are gained. Clear and continuous electron density is present for the reactive centre loop region P12 to P14 inserting into the top of the A-beta-sheet. Areas of the extended amino terminus, unique to antithrombin and important in the binding of the glycosaminoglycan heparin, can now be traced further than in the earlier structures. As in the earlier studies, the crystals contain one active and one latent molecule per asymmetric unit. Better definition of the electron density surrounding the D-helix and of the residues implicated in the binding of the heparin pentasaccharide (Arg47, Lys114, Lys125, Arg129) provides an insight into the change of affinity of binding that accompanies the change in conformation. In particular, the observed hydrogen bonding of these residues to the body of the molecule in the latent form explains the mechanism for the release of newly formed antithrombin-protease complexes into the circulation for catabolic removal. |
==About this Structure== | ==About this Structure== | ||
| - | 1E04 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 MAN, PO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1E04 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=MAN:'>MAN</scene>, <scene name='pdbligand=PO4:'>PO4</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=1E04 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Abrahams, J | + | [[Category: Abrahams, J P.]] |
| - | [[Category: Carrell, R | + | [[Category: Carrell, R W.]] |
| - | [[Category: Mccoy, A | + | [[Category: Mccoy, A J.]] |
| - | [[Category: Pei, X | + | [[Category: Pei, X Y.]] |
[[Category: Skinner, R.]] | [[Category: Skinner, R.]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
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[[Category: serpin]] | [[Category: serpin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:22:19 2008'' |
Revision as of 10:22, 21 February 2008
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PLASMA BETA ANTITHROMBIN-III
Overview
The crystal structure of a dimeric form of intact antithrombin has been solved to 2.6 A, representing the highest-resolution structure of an active, inhibitory serpin to date. The crystals were grown under microgravity conditions on Space Shuttle mission STS-67. The overall confidence in the structure, determined earlier from lower resolution data, is increased and new insights into the structure-function relationship are gained. Clear and continuous electron density is present for the reactive centre loop region P12 to P14 inserting into the top of the A-beta-sheet. Areas of the extended amino terminus, unique to antithrombin and important in the binding of the glycosaminoglycan heparin, can now be traced further than in the earlier structures. As in the earlier studies, the crystals contain one active and one latent molecule per asymmetric unit. Better definition of the electron density surrounding the D-helix and of the residues implicated in the binding of the heparin pentasaccharide (Arg47, Lys114, Lys125, Arg129) provides an insight into the change of affinity of binding that accompanies the change in conformation. In particular, the observed hydrogen bonding of these residues to the body of the molecule in the latent form explains the mechanism for the release of newly formed antithrombin-protease complexes into the circulation for catabolic removal.
About this Structure
1E04 is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.
Reference
The 2.6 A structure of antithrombin indicates a conformational change at the heparin binding site., Skinner R, Abrahams JP, Whisstock JC, Lesk AM, Carrell RW, Wardell MR, J Mol Biol. 1997 Feb 28;266(3):601-9. PMID:9067613
Page seeded by OCA on Thu Feb 21 12:22:19 2008
Categories: Homo sapiens | Single protein | Abrahams, J P. | Carrell, R W. | Mccoy, A J. | Pei, X Y. | Skinner, R. | GOL | MAN | PO4 | Serpin
