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.


2v3p

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2v3p.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2v3p.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2v3p| PDB=2v3p | SCENE= }}
{{STRUCTURE_2v3p| PDB=2v3p | SCENE= }}
-
'''CRYSTALLOGRAPHIC ANALYSIS OF BETA-AXIAL LIGAND SUBSTITUTIONS IN COBALAMIN BOUND TO TRANSCOBALAMIN'''
+
===CRYSTALLOGRAPHIC ANALYSIS OF BETA-AXIAL LIGAND SUBSTITUTIONS IN COBALAMIN BOUND TO TRANSCOBALAMIN===
-
==Overview==
+
<!--
-
Cobalamin (Cbl, vitamin B12) is an essential micronutrient that is synthesized only by bacteria. Mammals have developed a complex system for internalization of this vitamin from the diet. Three binding proteins (haptocorrin, intrinsic factor, transcobalamin (TC)) and several specific cell surface receptors are involved in the process of intestinal absorption, plasma transport and cellular uptake. The recent literature on the binding proteins is briefly reviewed. A structural study is presented addressing a unique feature of TC among the three proteins, i.e., the displacement of the weak Co(III)-ligand H2O at the upper (or beta) axial side of H2O-Cbl by a histidine side chain. We have investigated crystallographically the beta-ligand exchange on Cbl bound to TC by crystallization of bovine holo-TC in the presence of either cyanide or sulfite. The resulting electron density maps show that the histidine side chain has been displaced by an exogenous ligand CN(-) or SO(3)(-2)to a lower extent than expected based on their higher affinity for Co and excess concentration with respect to histidine. This may reflect either reduced affinities of CN(-) and SO(3)(-2)or the advantageous binding of the protein-integrated His-residue when competing for the beta-site of Cbl bound to TC. The loop hosting the histidine residue appears more flexible after disruption of the coordination bond His-Cbl but no other differences are observed in the overall structure of holo-TC. These structural results are discussed in relation to a possible physiological role of histidine substitution for H2O and regarding the role of beta-conjugated Cbl-analogues recently proposed for targeted delivery of imaging agents.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17943552}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17943552 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17943552}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Transport protein]]
[[Category: Transport protein]]
[[Category: Vitamin b12 transport protein]]
[[Category: Vitamin b12 transport protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 16 23:08:50 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:31:16 2008''

Revision as of 15:31, 28 July 2008

Image:2v3p.png

Template:STRUCTURE 2v3p

CRYSTALLOGRAPHIC ANALYSIS OF BETA-AXIAL LIGAND SUBSTITUTIONS IN COBALAMIN BOUND TO TRANSCOBALAMIN

Template:ABSTRACT PUBMED 17943552

About this Structure

2V3P is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Vitamin B12 transport proteins: crystallographic analysis of beta-axial ligand substitutions in cobalamin bound to transcobalamin., Wuerges J, Geremia S, Fedosov SN, Randaccio L, IUBMB Life. 2007 Nov;59(11):722-9. PMID:17943552

Page seeded by OCA on Mon Jul 28 18:31:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2v3p"
Personal tools