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.


1uvs

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1uvs.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1uvs.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1uvs| PDB=1uvs | SCENE= }}
{{STRUCTURE_1uvs| PDB=1uvs | SCENE= }}
-
'''BOVINE THROMBIN--BM51.1011 COMPLEX'''
+
===BOVINE THROMBIN--BM51.1011 COMPLEX===
-
==Overview==
+
<!--
-
BACKGROUND: The explosive growth in the rate of X-ray determination of protein structures is fuelled largely by the expectation that structural information will be useful for pharmacological and biotechnological applications. For example, there have been intensive efforts to develop orally administrable antithrombotic drugs using information about the crystal structures of blood coagulation factors, including thrombin. Most of the low molecular weight thrombin inhibitors studied so far are based on arginine and benzamidine. We sought to expand the database of information on thrombin-inhibitor binding by studying new classes of inhibitors. RESULTS: We report the structures of three new inhibitors complexed with thrombin, two based on 4-aminopyridine and one based on naphthamidine. We observe several geometry changes in the protein main chain and side chains which accompany inhibitor binding. The two inhibitors based on 4-aminopyridine bind in notably different ways: one forms a water-mediated hydrogen bond to the active site Ser195, the other induces a rotation of the Ser214-Trp215 peptide plane that is unprecedented in thrombin structures. These binding modes also differ in their 'weak' interactions, including CH-O hydrogen bonds and interactions between water molecules and aromatic pi-clouds. Induced-fit structural changes were also seen in the structure of the naphthamidine inhibitor complex. CONCLUSIONS: Protein flexibility and variable water structures are essential elements in protein-ligand interactions. Ligand design strategies that fail to take this into account may overlook or underestimate the potential of lead structures. Further, the significance of 'weak' interactions must be considered both in crystallographic refinement and in analysis of binding mechanisms.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8939759}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8939759 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8939759}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Serine protease]]
[[Category: Serine protease]]
[[Category: Thrombin]]
[[Category: Thrombin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:45:04 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:27:52 2008''

Revision as of 08:27, 28 July 2008

Image:1uvs.png

Template:STRUCTURE 1uvs

BOVINE THROMBIN--BM51.1011 COMPLEX

Template:ABSTRACT PUBMED 8939759

About this Structure

1UVS is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Enzyme flexibility, solvent and 'weak' interactions characterize thrombin-ligand interactions: implications for drug design., Engh RA, Brandstetter H, Sucher G, Eichinger A, Baumann U, Bode W, Huber R, Poll T, Rudolph R, von der Saal W, Structure. 1996 Nov 15;4(11):1353-62. PMID:8939759

Page seeded by OCA on Mon Jul 28 11:27:52 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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