2pw8: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /> <applet load="2pw8" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pw8, resolution 1.840Å" /> '''Crystal structure ...
 
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:2pw8.gif|left|200px]]<br />
[[Image:2pw8.jpg|left|200px]]<br /><applet load="2pw8" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="2pw8" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="2pw8, resolution 1.840&Aring;" />
caption="2pw8, resolution 1.840&Aring;" />
'''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 &gt;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 &gt;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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2PW8 OCA].  
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://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:27:43 2007''
''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

File:2pw8.jpg


2pw8, resolution 1.840Å

Drag the structure with the mouse to rotate

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 NI and NA 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

Proteopedia Page Contributors and Editors (what is this?)

OCA