We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2o84

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2o84.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2o84.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2o84| PDB=2o84 | SCENE= }}
{{STRUCTURE_2o84| PDB=2o84 | SCENE= }}
-
'''Crystal structure of K206E mutant of N-lobe human transferrin'''
+
===Crystal structure of K206E mutant of N-lobe human transferrin===
-
==Overview==
+
<!--
-
Iron uptake by humans depends on the ability of the serum protein transferrin (Tf) to bind iron as Fe(3+) with high affinity but reversibly. Iron release into cells occurs through receptor-mediated endocytosis, aided by the lower endosomal pH of about 5.5. The protonation of a hydrogen-bonded pair of lysines, Lys206 and Lys296, adjacent to the N-lobe iron site of Tf has been proposed to create a repulsive interaction that stimulates domain opening and iron release. The crystal structures of two mutants, K206E (in which Lys206 is mutated to Glu) and K206E/K296E (in which both lysines are mutated to Glu), have been determined. The K206E structure (2.6 A resolution; R = 0.213, R(free) = 0.269) shows that a salt bridge is formed between Glu206 and Lys296, thus explaining the drastically slower iron release by this mutant. The K206E/K296E double-mutant structure (2.8 A resolution; R = 0.232, R(free) = 0.259) shows that the Glu296 side chain moves away from Glu206, easing any repulsive interaction and instead interacting with the iron ligand His249. The evident conformational flexibility is consistent with an alternative model for the operation of the dilysine pair in iron release in which it facilitates concerted proton transfer to the tyrosine ligand Tyr188 as one step in the weakening of iron binding.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17327678}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17327678 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17327678}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Human transferrin]]
[[Category: Human transferrin]]
[[Category: Iron binding and release]]
[[Category: Iron binding and release]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:26:25 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:18:39 2008''

Revision as of 00:18, 28 July 2008

Image:2o84.png

Template:STRUCTURE 2o84

Crystal structure of K206E mutant of N-lobe human transferrin

Template:ABSTRACT PUBMED 17327678

About this Structure

2O84 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structures of two mutants that probe the role in iron release of the dilysine pair in the N-lobe of human transferrin., Baker HM, Nurizzo D, Mason AB, Baker EN, Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):408-14. Epub 2007, Feb 21. PMID:17327678

Page seeded by OCA on Mon Jul 28 03:18:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2o84"
Personal tools