This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2pw8
From Proteopedia
(New page: 200px<br /> <applet load="2pw8" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pw8, resolution 1.840Å" /> '''Crystal structure ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2pw8. | + | [[Image:2pw8.jpg|left|200px]]<br /><applet load="2pw8" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2pw8" size=" | + | |
caption="2pw8, resolution 1.840Å" /> | caption="2pw8, resolution 1.840Å" /> | ||
'''Crystal structure of sulfo-hirudin complexed to thrombin'''<br /> | '''Crystal structure of sulfo-hirudin complexed to thrombin'''<br /> | ||
| Line 6: | Line 5: | ||
==Overview== | ==Overview== | ||
The leech-derived anticoagulant hirudin is post-translationally sulfated, on tyrosine 63, resulting in a >10-fold increase in its affinity for, thrombin. We report the structure of a biosynthetic sulfo-hirudin, complexed to thrombin solved to 1.84 A resolution and show that sulfation, is responsible for a salt bridge and an extended hydrogen-bond network, that taken together account for the increased affinity of sulfo-hirudin, for thrombin. We also identify a divalent cation binding site at the, interface between the two subunits of alpha-thrombin that may modulate the, physiological activity of thrombin. | The leech-derived anticoagulant hirudin is post-translationally sulfated, on tyrosine 63, resulting in a >10-fold increase in its affinity for, thrombin. We report the structure of a biosynthetic sulfo-hirudin, complexed to thrombin solved to 1.84 A resolution and show that sulfation, is responsible for a salt bridge and an extended hydrogen-bond network, that taken together account for the increased affinity of sulfo-hirudin, for thrombin. We also identify a divalent cation binding site at the, interface between the two subunits of alpha-thrombin that may modulate the, physiological activity of thrombin. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: Dysprothrombinemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176930 176930]], Hyperprothrombinemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176930 176930]], Hypoprothrombinemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176930 176930]] | ||
==About this Structure== | ==About this Structure== | ||
| - | 2PW8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NI and NA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2PW8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NI:'>NI</scene> and <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PW8 OCA]. |
==Reference== | ==Reference== | ||
| Line 29: | Line 25: | ||
[[Category: thrombin]] | [[Category: thrombin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:33:46 2008'' |
Revision as of 10:33, 23 January 2008
|
Crystal structure of sulfo-hirudin complexed to thrombin
Overview
The leech-derived anticoagulant hirudin is post-translationally sulfated, on tyrosine 63, resulting in a >10-fold increase in its affinity for, thrombin. We report the structure of a biosynthetic sulfo-hirudin, complexed to thrombin solved to 1.84 A resolution and show that sulfation, is responsible for a salt bridge and an extended hydrogen-bond network, that taken together account for the increased affinity of sulfo-hirudin, for thrombin. We also identify a divalent cation binding site at the, interface between the two subunits of alpha-thrombin that may modulate the, physiological activity of thrombin.
About this Structure
2PW8 is a Protein complex structure of sequences from Hirudo medicinalis and Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal Structure of a Biosynthetic Sulfo-hirudin Complexed to Thrombin., Liu CC, Brustad E, Liu W, Schultz PG, J Am Chem Soc. 2007 Aug 9;. PMID:17685615
Page seeded by OCA on Wed Jan 23 12:33:46 2008
Categories: Hirudo medicinalis | Homo sapiens | Protein complex | Brustad, E. | Liu, C.C. | Liu, W. | Schultz, P.G. | NA | NI | Hirudin | Hydrolase | Sulfotyrosine | Thrombin
