We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2thf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2thf.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2thf.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2thf| PDB=2thf | SCENE= }}
{{STRUCTURE_2thf| PDB=2thf | SCENE= }}
-
'''STRUCTURE OF HUMAN ALPHA-THROMBIN Y225F MUTANT BOUND TO D-PHE-PRO-ARG-CHLOROMETHYLKETONE'''
+
===STRUCTURE OF HUMAN ALPHA-THROMBIN Y225F MUTANT BOUND TO D-PHE-PRO-ARG-CHLOROMETHYLKETONE===
-
==Overview==
+
<!--
-
Residue 225 in serine proteases of the chymotrypsin family is Pro or Tyr in more than 95% of nearly 300 available sequences. Proteases with Y225 (like some blood coagulation and complement factors) are almost exclusively found in vertebrates, whereas proteases with P225 (like degradative enzymes) are present from bacteria to human. Saturation mutagenesis of Y225 in thrombin shows that residue 225 affects ligand recognition up to 60,000-fold. With the exception of Tyr and Phe, all residues are associated with comparable or greatly reduced catalytic activity relative to Pro. The crystal structures of three mutants that differ widely in catalytic activity (Y225F, Y225P, and Y225I) show that although residue 225 makes no contact with substrate, it drastically influences the shape of the water channel around the primary specificity site. The activity profiles obtained for thrombin also suggest that the conversion of Pro to Tyr or Phe documented in the vertebrates occurred through Ser and was driven by a significant gain (up to 50-fold) in catalytic activity. In fact, Ser and Phe are documented in 4% of serine proteases, which together with Pro and Tyr account for almost the entire distribution of residues at position 225. The unexpected crucial role of residue 225 in serine proteases explains the evolutionary selection of residues at this position and shows that the structural determinants of protease activity and specificity are more complex than currently believed. These findings have broad implications in the rational design of enzymes with enhanced catalytic properties.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10051558}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10051558 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10051558}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Waksman, G.]]
[[Category: Waksman, G.]]
[[Category: Serine protease]]
[[Category: Serine protease]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:23:55 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:57:27 2008''

Revision as of 17:57, 27 July 2008

Image:2thf.png

Template:STRUCTURE 2thf

STRUCTURE OF HUMAN ALPHA-THROMBIN Y225F MUTANT BOUND TO D-PHE-PRO-ARG-CHLOROMETHYLKETONE

Template:ABSTRACT PUBMED 10051558

About this Structure

2THF is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Unexpected crucial role of residue 225 in serine proteases., Guinto ER, Caccia S, Rose T, Futterer K, Waksman G, Di Cera E, Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):1852-7. PMID:10051558

Page seeded by OCA on Sun Jul 27 20:57:27 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2thf"
Personal tools