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.


1p1g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1p1g.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1p1g.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1p1g| PDB=1p1g | SCENE= }}
{{STRUCTURE_1p1g| PDB=1p1g | SCENE= }}
-
'''MACROPHAGE MIGRATION INHIBITORY FACTOR (MIF) WITH PRO-1 MUTATED TO GLY-1'''
+
===MACROPHAGE MIGRATION INHIBITORY FACTOR (MIF) WITH PRO-1 MUTATED TO GLY-1===
-
==Overview==
+
<!--
-
Macrophage migration inhibitory factor (MIF) is an important immunoregulatory molecule with a unique ability to suppress the anti-inflammatory effects of glucocorticoids. Although considered a cytokine, MIF possesses a three-dimensional structure and active site similar to those of 4-oxalocrotonate tautomerase and 5-carboxymethyl-2-hydroxymuconate isomerase. Moreover, a number of catalytic activities have been defined for MIF. To gain insight into the role of catalysis in the biological function of MIF, we have begun to characterize the catalytic activities in more detail. Here we report the crystal structure of MIF complexed with p-hydroxyphenylpyruvate, a substrate for the phenylpyruvate tautomerase activity of MIF. The three binding sites for p-hydroxyphenylpyruvate in the MIF trimer lie at the interface between two subunits. The substrate interacts with Pro-1, Lys-32, and Ile-64 from one subunit and Tyr-95 and Asn-97 from an adjacent subunit. Pro-1 is positioned to function as a catalytic base. There is no functional group that polarizes the alpha-carbonyl of the substrate to weaken the adjacent C-H bond. Mutation of Pro-1 to glycine substantially reduces the catalytic activity. The insertion of an alanine between Pro-1 and Met-2 essentially abolishes activity. Structural studies of these mutants define a source of the reduced activity and provide insight into the mechanism of the catalytic reaction.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10353846}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10353846 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10353846}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Enzyme]]
[[Category: Enzyme]]
[[Category: Protein hormone]]
[[Category: Protein hormone]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:33:47 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:58:18 2008''

Revision as of 16:58, 27 July 2008

Image:1p1g.png

Template:STRUCTURE 1p1g

MACROPHAGE MIGRATION INHIBITORY FACTOR (MIF) WITH PRO-1 MUTATED TO GLY-1

Template:ABSTRACT PUBMED 10353846

About this Structure

1P1G is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Pro-1 of macrophage migration inhibitory factor functions as a catalytic base in the phenylpyruvate tautomerase activity., Lubetsky JB, Swope M, Dealwis C, Blake P, Lolis E, Biochemistry. 1999 Jun 1;38(22):7346-54. PMID:10353846

Page seeded by OCA on Sun Jul 27 19:58:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1p1g"
Personal tools