We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1t1f

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1t1f.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1t1f.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1t1f| PDB=1t1f | SCENE= }}
{{STRUCTURE_1t1f| PDB=1t1f | SCENE= }}
-
'''Crystal Structure of Native Antithrombin in its Monomeric Form'''
+
===Crystal Structure of Native Antithrombin in its Monomeric Form===
-
==Overview==
+
<!--
-
The poor inhibitory activity of circulating antithrombin (AT) is critical to the formation of blood clots at sites of vascular damage. AT becomes an efficient inhibitor of the coagulation proteases only after binding to a specific heparin pentasaccharide, which alters the conformation of the reactive center loop (RCL). The molecular basis of this activation event lies at the heart of the regulation of hemostasis and accounts for the anticoagulant properties of the low molecular weight heparins. Although several structures of AT have been solved, the conformation of the RCL in native AT remains unknown because of the obligate crystal contact between the RCL of native AT and its latent counterpart. Here we report the crystallographic structure of a variant of AT in its monomeric native state. The RCL shifted approximately 20 A, and a salt bridge was observed between the P1 residue (Arg-393) and Glu-237. This contact explains the effect of mutations at the P1 position on the affinity of AT for heparin and also the properties of AT-Truro (E237K). The relevance of the observed conformation was verified through mutagenesis studies and by solving structures of the same variant in different crystal forms. We conclude that the poor inhibitory activity of the circulating form of AT is partially conferred by intramolecular contacts that restrain the RCL, orient the P1 residue away from attacking proteases, and additionally block the exosite utilized in protease recognition.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16973611}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16973611 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16973611}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Thrombin]]
[[Category: Thrombin]]
[[Category: X-ray crystallography]]
[[Category: X-ray crystallography]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:23:10 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:07:29 2008''

Revision as of 01:07, 28 July 2008

Image:1t1f.png

Template:STRUCTURE 1t1f

Crystal Structure of Native Antithrombin in its Monomeric Form

Template:ABSTRACT PUBMED 16973611

About this Structure

1T1F is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of monomeric native antithrombin reveals a novel reactive center loop conformation., Johnson DJ, Langdown J, Li W, Luis SA, Baglin TP, Huntington JA, J Biol Chem. 2006 Nov 17;281(46):35478-86. Epub 2006 Sep 13. PMID:16973611

Page seeded by OCA on Mon Jul 28 04:07:29 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1t1f"
Personal tools