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.


1bda

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1bda.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1bda.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1bda| PDB=1bda | SCENE= }}
{{STRUCTURE_1bda| PDB=1bda | SCENE= }}
-
'''CATALYTIC DOMAIN OF HUMAN SINGLE CHAIN TISSUE PLASMINOGEN ACTIVATOR IN COMPLEX WITH DANSYL-EGR-CMK (DANSYL-GLU-GLY-ARG CHLOROMETHYL KETONE)'''
+
===CATALYTIC DOMAIN OF HUMAN SINGLE CHAIN TISSUE PLASMINOGEN ACTIVATOR IN COMPLEX WITH DANSYL-EGR-CMK (DANSYL-GLU-GLY-ARG CHLOROMETHYL KETONE)===
-
==Overview==
+
<!--
-
Tissue type plasminogen activator (tPA) is the physiological initiator of fibrinolysis, activating plasminogen via highly specific proteolysis; plasmin then degrades fibrin with relatively broad specificity. Unlike other chymotrypsin family serine proteinases, tPA is proteolytically active in a single-chain form. This form is also preferred for therapeutic administration of tPA in cases of acute myocardial infarction. The proteolytic cleavage which activates most other chymotrypsin family serine proteinases increases the catalytic efficiency of tPA only 5- to 10-fold. The X-ray crystal structure of the catalytic domain of recombinant human single-chain tPA shows that Lys156 forms a salt bridge with Asp194, promoting an active conformation in the single-chain form. Comparisons with the structures of other serine proteinases that also possess Lys156, such as trypsin, factor Xa and human urokinase plasminogen activator (uPA), identify a set of secondary interactions which are required for Lys156 to fulfil this activating role. These findings help explain the anomalous single-chain activity of tPA and may suggest strategies for design of new therapeutic plasminogen activators.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9305622}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9305622 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9305622}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Plasminogen activator]]
[[Category: Plasminogen activator]]
[[Category: Trypsin like serine protease]]
[[Category: Trypsin like serine protease]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:21:56 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:52:59 2008''

Revision as of 15:53, 30 June 2008

Image:1bda.png

Template:STRUCTURE 1bda

CATALYTIC DOMAIN OF HUMAN SINGLE CHAIN TISSUE PLASMINOGEN ACTIVATOR IN COMPLEX WITH DANSYL-EGR-CMK (DANSYL-GLU-GLY-ARG CHLOROMETHYL KETONE)

Template:ABSTRACT PUBMED 9305622

About this Structure

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

Reference

Lysine 156 promotes the anomalous proenzyme activity of tPA: X-ray crystal structure of single-chain human tPA., Renatus M, Engh RA, Stubbs MT, Huber R, Fischer S, Kohnert U, Bode W, EMBO J. 1997 Aug 15;16(16):4797-805. PMID:9305622

Page seeded by OCA on Mon Jun 30 18:52:59 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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