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.

2ant

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2ant.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2ant.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2ant| PDB=2ant | SCENE= }}
{{STRUCTURE_2ant| PDB=2ant | SCENE= }}
-
'''THE 2.6 A STRUCTURE OF ANTITHROMBIN INDICATES A CONFORMATIONAL CHANGE AT THE HEPARIN BINDING SITE'''
+
===THE 2.6 A STRUCTURE OF ANTITHROMBIN INDICATES A CONFORMATIONAL CHANGE AT THE HEPARIN BINDING SITE===
-
==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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9067613}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9067613 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9067613}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Inhibitor]]
[[Category: Inhibitor]]
[[Category: Serpin]]
[[Category: Serpin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:16:03 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:29:47 2008''

Revision as of 07:30, 29 July 2008

Image:2ant.png

Template:STRUCTURE 2ant

THE 2.6 A STRUCTURE OF ANTITHROMBIN INDICATES A CONFORMATIONAL CHANGE AT THE HEPARIN BINDING SITE

Template:ABSTRACT PUBMED 9067613

About this Structure

2ANT is a Single protein structure of sequence from Homo sapiens. 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 Tue Jul 29 10:29:47 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ant"
Personal tools