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.


32c2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:32c2.gif|left|200px]]
+
{{Seed}}
 +
[[Image:32c2.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_32c2| PDB=32c2 | SCENE= }}
{{STRUCTURE_32c2| PDB=32c2 | SCENE= }}
-
'''STRUCTURE OF AN ACTIVITY SUPPRESSING FAB FRAGMENT TO CYTOCHROME P450 AROMATASE'''
+
===STRUCTURE OF AN ACTIVITY SUPPRESSING FAB FRAGMENT TO CYTOCHROME P450 AROMATASE===
-
==Overview==
+
<!--
-
The crystal structure of a Fab fragment (Fab3-2C2) of a monoclonal antibody raised against aromatase cytochrome P450 P450arom) has been determined at 3.0 A resolution. P450arom is a membrane bound enzyme responsible for the catalysis of indrogens to estrogens, the process of aromatization, and hence has been implicated in hormone-dependent breast cancer. The Fab fragment of MAb3-2C2 IgG suppresses P450arom activity in a dose dependent manner. The Fab3-2C2 molecule crystallizes n the space group P2(1)2(1)2(1) with a unit cell of a= 154.89 A, b = 73.51 A, and c= 36.90 A. The crystal structure consists of a light and a heavy chain in the asymmetric unit, each characterized by the greek-key antiparallel beta barrel folding seen in all Fab structures. The average elbow angle between the two domains is 143 degrees. Modeling of the interactions between the variable domains of the antibody and a known model of P450arom maps the epitope to a region of the enzyme that is consistent with the available biochemical data and the activity-suppressing function of the antibody. The epitope mapping result is further supported by the inability of MAb3-2C2 IgG to suppress the activity of, or to interact with placental porcine P450arom, which is 81% identical (86% similar) to human P450arom but has a few key substitutions in the putative epitope region.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10449095}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10449095 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10449095}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Fab]]
[[Category: Fab]]
[[Category: P450]]
[[Category: P450]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:15:58 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:49:43 2008''

Revision as of 07:49, 29 July 2008

Image:32c2.png

Template:STRUCTURE 32c2

STRUCTURE OF AN ACTIVITY SUPPRESSING FAB FRAGMENT TO CYTOCHROME P450 AROMATASE

Template:ABSTRACT PUBMED 10449095

About this Structure

Full crystallographic information is available from OCA.

Reference

Structure of an activity suppressing Fab fragment to cytochrome P450 aromatase: insights into the antibody-antigen interactions., Sawicki MW, Ng PC, Burkhart BM, Pletnev VZ, Higashiyama T, Osawa Y, Ghosh D, Mol Immunol. 1999 May;36(7):423-32. PMID:10449095

Page seeded by OCA on Tue Jul 29 10:49:43 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/32c2"
Personal tools