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.


1hrt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1hrt.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1hrt.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hrt| PDB=1hrt | SCENE= }}
{{STRUCTURE_1hrt| PDB=1hrt | SCENE= }}
-
'''THE STRUCTURE OF A COMPLEX OF BOVINE ALPHA-THROMBIN AND RECOMBINANT HIRUDIN AT 2.8 ANGSTROMS RESOLUTION'''
+
===THE STRUCTURE OF A COMPLEX OF BOVINE ALPHA-THROMBIN AND RECOMBINANT HIRUDIN AT 2.8 ANGSTROMS RESOLUTION===
-
==Overview==
+
<!--
-
Crystals of the complex of bovine alpha-thrombin with recombinant hirudin variant 1 have space group C222(1) with cell constants a = 59.11, b = 102.62, and c = 143.26 A. The orientation and position of the thrombin component was determined by molecular replacement and the hirudin molecule was fit in 2 magnitude of Fo - magnitude of Fc electron density maps. The structure was refined by restrained least squares and simulated annealing to R = 0.161 at 2.8-A resolution. The binding of hirudin to thrombin is generally similar to that observed in the crystals of human thrombin-hirudin. Several differences in the interactions of the COOH-terminal polypeptide of hirudin, specifically of residues Asp-55h, Phe-56h, Glu-57h, and Glu-58h, and a few differences in the interactions of the hirudin core, specifically of residues Asp-5h, Ser-19h, and Asn-20h, with thrombin from human thrombin-hirudin suggest that there is some flexibility in the binding of these 2 molecules. Most of the residues in the 9 subsites that bind fibrinopeptide A7-16 to thrombin also interact with the NH2-terminal domain of hirudin. The S1 subsite is a notable exception in that only 1 of its 6 residues, namely Ser-214, interacts with hirudin. The only difference between human and bovine thrombins that appears to influence the binding of hirudin is the replacement of Lys-149E by an acidic glutamate in the bovine enzyme.
+
The line below this paragraph, {{ABSTRACT_PUBMED_1517214}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 1517214 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_1517214}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Edwards, B F.P.]]
[[Category: Edwards, B F.P.]]
[[Category: Vitali, J.]]
[[Category: Vitali, J.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:10:15 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:35:58 2008''

Revision as of 05:36, 1 July 2008

Image:1hrt.png

Template:STRUCTURE 1hrt

THE STRUCTURE OF A COMPLEX OF BOVINE ALPHA-THROMBIN AND RECOMBINANT HIRUDIN AT 2.8 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 1517214

About this Structure

1HRT is a Protein complex structure of sequences from Bos taurus and Hirudo medicinalis. Full crystallographic information is available from OCA.

Reference

The structure of a complex of bovine alpha-thrombin and recombinant hirudin at 2.8-A resolution., Vitali J, Martin PD, Malkowski MG, Robertson WD, Lazar JB, Winant RC, Johnson PH, Edwards BF, J Biol Chem. 1992 Sep 5;267(25):17670-8. PMID:1517214

Page seeded by OCA on Tue Jul 1 08:35:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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