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.


1erb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1erb.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1erb.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1erb| PDB=1erb | SCENE= }}
{{STRUCTURE_1erb| PDB=1erb | SCENE= }}
-
'''THE INTERACTION OF N-ETHYL RETINAMIDE WITH PLASMA RETINOL-BINDING PROTEIN (RBP) AND THE CRYSTAL STRUCTURE OF THE RETINOID-RBP COMPLEX AT 1.9 ANGSTROMS RESOLUTION'''
+
===THE INTERACTION OF N-ETHYL RETINAMIDE WITH PLASMA RETINOL-BINDING PROTEIN (RBP) AND THE CRYSTAL STRUCTURE OF THE RETINOID-RBP COMPLEX AT 1.9 ANGSTROMS RESOLUTION===
-
==Overview==
+
<!--
-
The three-dimensional structure of bovine plasma retinol-binding protein (RBP) complexed with N-ethyl retinamide has been determined at 1.9-A resolution. The crystals of the complex (space group P2(1)2(1)2(1), a = 46.27, b = 49.11, c = 76.41 A) are isomorphous with those of bovine holo and apoRBP. The final crystallographic R factor is 0.172 for 11,261 observed reflections. The model of the retinoid-RBP complex is nearly identical to that of bovine retinol-RBP complex; the root mean square deviations between the alpha-carbons in the two proteins is 0.15 A. The N-ethyl retinamide molecule fits in the beta-barrel in the same position previously occupied by the vitamin. The ethyl group of the retinoid replaces the retinol hydroxyl group and a water molecule hydrogen bonded to it. This substitution has no consequence on the overall conformation of the protein. The modification of the functional end group of retinol does not lead to an apparent loss of affinity of the retinol analog for apoRBP, as established by means of fluorometric titrations with N-ethyl retinamide. However, the binding of the retinoid to RBP abolishes or greatly reduces the affinity of RBP for transthyretin. This behavior further supports the hypothesis that the area of the entrance of the beta-barrel, which includes the ethyl group of the retinoid bound to RBP, is involved in the interaction with transthyretin. Moreover, it indicates a high degree of complementarity of interacting surfaces between RBP and transthyretin. In fact, the replacement of the retinol hydroxyl group and quite small structural changes in the above region of the RBP molecule drastically affect the protein-protein recognition.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8227049}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8227049 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8227049}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Zanotti, G.]]
[[Category: Zanotti, G.]]
[[Category: Retinol transport]]
[[Category: Retinol transport]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:25:52 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 01:44:58 2008''

Revision as of 22:45, 30 June 2008

Image:1erb.png

Template:STRUCTURE 1erb

THE INTERACTION OF N-ETHYL RETINAMIDE WITH PLASMA RETINOL-BINDING PROTEIN (RBP) AND THE CRYSTAL STRUCTURE OF THE RETINOID-RBP COMPLEX AT 1.9 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 8227049

About this Structure

1ERB is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

The interaction of N-ethyl retinamide with plasma retinol-binding protein (RBP) and the crystal structure of the retinoid-RBP complex at 1.9-A resolution., Zanotti G, Malpeli G, Berni R, J Biol Chem. 1993 Nov 25;268(33):24873-9. PMID:8227049

Page seeded by OCA on Tue Jul 1 01:44:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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