1l4d: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1l4d.gif|left|200px]]
{{Seed}}
[[Image:1l4d.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1l4d|  PDB=1l4d  |  SCENE=  }}  
{{STRUCTURE_1l4d|  PDB=1l4d  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF MICROPLASMINOGEN-STREPTOKINASE ALPHA DOMAIN COMPLEX'''
===CRYSTAL STRUCTURE OF MICROPLASMINOGEN-STREPTOKINASE ALPHA DOMAIN COMPLEX===




==Overview==
<!--
Streptokinase (SK) is a thrombolytic agent widely used for the clinical treatment of clotting disorders such as heart attack. The treatment is based on the ability of SK to bind plasminogen (Pg) or plasmin (Pm), forming complexes that proteolytically activate other Pg molecules to Pm, which carries out fibrinolysis. SK contains three major domains. The N-terminal domain, SKalpha, provides the complex with substrate recognition towards Pg. SKalpha contains a unique mobile loop, residues 45-70, absent in the corresponding domains of other bacterial Pg activators. To study the roles of this loop, we deleted 12 residues in this loop in both full-length SK and the SKalpha fragment. Kinetic data indicate that this loop participates in the recognition of substrate Pg, but does not function in the active site formation in the activator complex. Two crystal structures of the deletion mutant of SKalpha (SKalpha(delta)) complexed with the protease domain of Pg were determined. While the structure of SKalpha(delta) is essentially the same as this domain in full-length SK, the mode of SK-Pg interaction was however different from a previously observed structure. Even though mutagenesis studies indicated that the current complex represents a minor interacting form in solution, the binding to SKalpha(delta) triggered similar conformational changes in the Pg active site in both crystal forms.
The line below this paragraph, {{ABSTRACT_PUBMED_12456874}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12456874 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_12456874}}


==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Streptokinase]]
[[Category: Streptokinase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:31:43 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:40:54 2008''

Revision as of 08:40, 2 July 2008

File:1l4d.png

Template:STRUCTURE 1l4d

CRYSTAL STRUCTURE OF MICROPLASMINOGEN-STREPTOKINASE ALPHA DOMAIN COMPLEX

Template:ABSTRACT PUBMED 12456874

About this Structure

1L4D is a Protein complex structure of sequences from Homo sapiens and Streptococcus dysgalactiae subsp. equisimilis. Full crystallographic information is available from OCA.

Reference

Effects of deletion of streptokinase residues 48-59 on plasminogen activation., Wakeham N, Terzyan S, Zhai P, Loy JA, Tang J, Zhang XC, Protein Eng. 2002 Sep;15(9):753-61. PMID:12456874

Page seeded by OCA on Wed Jul 2 11:40:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1l4d&oldid=623882"