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.


4htc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:4htc.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:4htc.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_4htc| PDB=4htc | SCENE= }}
{{STRUCTURE_4htc| PDB=4htc | SCENE= }}
-
'''THE REFINED STRUCTURE OF THE HIRUDIN-THROMBIN COMPLEX'''
+
===THE REFINED STRUCTURE OF THE HIRUDIN-THROMBIN COMPLEX===
-
==Overview==
+
<!--
-
The structure of a recombinant hirudin (variant 2, Lys47) human alpha-thrombin complex has been refined using restrained least-squares methods to a crystallographic R-factor of 0.173. The hirudin structure consists of an N-terminal domain folded into a globular unit and a long 17-peptide C-terminal in an extended chain conformation. The N-terminal domain binds at the active-site of thrombin where Ile1' to Tyr3' penetrates to the catalytic triad. The alpha-amino group of Ile1' of hirudin makes a hydrogen bond with OG of Ser195 of thrombin, the side-chains of Ile1' and Tyr3' occupy the apolar site, Thr2' is at the entrance to, but does not enter, the S1 specificity site and Ile1' to Tyr3' form a parallel beta-strand with Ser214 to Gly219. The latter interaction is antiparallel in all other serine proteinase-protein inhibitor complexes. The extended C-terminal segment of hirudin, which is abundant in acidic residues, makes many electrostatic interactions with the fibrinogen binding exosite while the last five residues are in a 3(10) helical turn residing in a hydrophobic patch on the thrombin surface. The precision of the complementarity displayed by these two molecules produces numerous interactions, which although independently generally weak, together are responsible for the high degree of affinity and specificity. Although hirudin-thrombin and D-Phe-Pro-Arg-chloromethyl ketone-thrombin differ in conformation in the autolysis loop (Lys145 to Gly150), this is most likely due to different crystal packing interactions and changes in circular dichroism between the two are probably due to the inherent flexibility of the loop. An RGD sequence, which is generally known to be involved in cell surface receptor interactions, occurs in thrombin and is associated with a long solvent channel filled with water molecules leading to the surface from the end of the S1 site. However, the RGD triplet does not appear to be able to interact in concert in a surface binding mode.
+
The line below this paragraph, {{ABSTRACT_PUBMED_1920434}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 1920434 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_1920434}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Rydel, T J.]]
[[Category: Rydel, T J.]]
[[Category: Tulinsky, A.]]
[[Category: Tulinsky, A.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:25:25 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:41:13 2008''

Revision as of 10:41, 3 July 2008

Image:4htc.png

Template:STRUCTURE 4htc

THE REFINED STRUCTURE OF THE HIRUDIN-THROMBIN COMPLEX

Template:ABSTRACT PUBMED 1920434

About this Structure

4HTC is a Protein complex structure of sequences from Hirudo medicinalis and Homo sapiens. Full crystallographic information is available from OCA.

Reference

Refined structure of the hirudin-thrombin complex., Rydel TJ, Tulinsky A, Bode W, Huber R, J Mol Biol. 1991 Sep 20;221(2):583-601. PMID:1920434

Page seeded by OCA on Thu Jul 3 13:41:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4htc"
Personal tools