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.




1dfp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1dfp.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1dfp.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1dfp| PDB=1dfp | SCENE= }}
{{STRUCTURE_1dfp| PDB=1dfp | SCENE= }}
-
'''FACTOR D INHIBITED BY DIISOPROPYL FLUOROPHOSPHATE'''
+
===FACTOR D INHIBITED BY DIISOPROPYL FLUOROPHOSPHATE===
-
==Overview==
+
<!--
-
Factor D (D) is a serine protease, crucial for the activation of the alternative complement pathway. Only a limited number of general serine protease inhibitors are known to inhibit D, most of which covalently bind to the serine hydroxyl of the catalytic triad. The structure of the first enzyme:inhibitor covalent adduct of D with diisopropyl fluorophosphate (DIP:D) to a resolution of 2.4 A is described. The inhibited enzyme is similar in overall structure to the native enzyme and to trypsin, yet exhibits notable differences in the active site. One region of the active site is conserved between D and trypsin with respect to amino-acid sequence and to conformation. Another reflects the amino-acid substitutions and conformational flexibility between these enzymes. The active-site histidine residue is observed in the gauche+ conformation, not the normal gauche- orientation seen in the classic catalytic triad arrangement required for enzymatic activity in serine proteases. Comparisons of the active sites between native D, the DIP:D adduct, and DIP-inhibited trypsin have provided fundamental insights currently being employed in the design of novel small-molecule pharmaceutical agents capable of modulating the alternative complement pathway.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15299948}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15299948 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15299948}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Serine protease]]
[[Category: Serine protease]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:48:12 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:00:36 2008''

Revision as of 20:00, 30 June 2008

Image:1dfp.png

Template:STRUCTURE 1dfp

FACTOR D INHIBITED BY DIISOPROPYL FLUOROPHOSPHATE

Template:ABSTRACT PUBMED 15299948

About this Structure

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

Reference

Structure of diisopropyl fluorophosphate-inhibited factor D., Cole LB, Chu N, Kilpatrick JM, Volanakis JE, Narayana SV, Babu YS, Acta Crystallogr D Biol Crystallogr. 1997 Mar 1;53(Pt 2):143-50. PMID:15299948

Page seeded by OCA on Mon Jun 30 23:00:36 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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