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.


1nnt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1nnt.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1nnt.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1nnt| PDB=1nnt | SCENE= }}
{{STRUCTURE_1nnt| PDB=1nnt | SCENE= }}
-
'''STRUCTURAL EVIDENCE FOR A PH-SENSITIVE DI-LYSINE TRIGGER IN THE HEN OVOTRANSFERRIN N-LOBE: IMPLICATIONS FOR TRANSFERRIN IRON RELEASE'''
+
===STRUCTURAL EVIDENCE FOR A PH-SENSITIVE DI-LYSINE TRIGGER IN THE HEN OVOTRANSFERRIN N-LOBE: IMPLICATIONS FOR TRANSFERRIN IRON RELEASE===
-
==Overview==
+
<!--
-
Members of the transferrin family of proteins are involved in Fe3+ transport (serum transferrins) and are also believed to possess antimicrobial activity (ovotransferrins and lactoferrins). The structure of the monoferric N-terminal half-molecule of hen ovotransferrin, reported here at 2.3-A resolution, reveals an unusual interdomain interaction formed between the side-chain NZ atoms of Lys 209 and Lys 301, which are 2.3 A apart. This strong interaction appears to be an example of a low-barrier hydrogen bond between the two lysine NZ atoms, both of which are also involved in a hydrogen-bonding interaction with the aromatic ring of a tyrosine residue. Crystals of the protein were grown at pH 5.9, which is well below the usual pKa approximately 10 for a lysine side chain. We suggest that the pKa of either one or both of these residues lies below the pH of the structure determination and is, therefore, not positively charged. This finding may serve to explain, on a molecular basis, the pH dependence of transferrin Fe3+ release. We propose that uptake of the Fe(3+)-transferrin complex into an acidic endosome (viz., pH approximately 5.0) via receptor-mediated endocytosis will result in the protonation of both lysine residues. The close proximity of the two resulting positive charges, and their location on opposite domains of the N-lobe, might well be the driving force that opens the two domains of the protein, exposing the Fe3+ ion and facilitating its release.(ABSTRACT TRUNCATED AT 250 WORDS)
+
The line below this paragraph, {{ABSTRACT_PUBMED_8218271}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8218271 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8218271}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Sacchettini, J C.]]
[[Category: Sacchettini, J C.]]
[[Category: Iron transport protein]]
[[Category: Iron transport protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:45:33 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:45:22 2008''

Revision as of 23:45, 28 July 2008

Image:1nnt.png

Template:STRUCTURE 1nnt

STRUCTURAL EVIDENCE FOR A PH-SENSITIVE DI-LYSINE TRIGGER IN THE HEN OVOTRANSFERRIN N-LOBE: IMPLICATIONS FOR TRANSFERRIN IRON RELEASE

Template:ABSTRACT PUBMED 8218271

About this Structure

1NNT is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

Structural evidence for a pH-sensitive dilysine trigger in the hen ovotransferrin N-lobe: implications for transferrin iron release., Dewan JC, Mikami B, Hirose M, Sacchettini JC, Biochemistry. 1993 Nov 16;32(45):11963-8. PMID:8218271

Page seeded by OCA on Tue Jul 29 02:45:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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