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.

1o9x

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1o9x.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1o9x.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1o9x| PDB=1o9x | SCENE= }}
{{STRUCTURE_1o9x| PDB=1o9x | SCENE= }}
-
'''HUMAN SERUM ALBUMIN COMPLEXED WITH TETRADECANOIC ACID (MYRISTIC ACID) AND HEMIN'''
+
===HUMAN SERUM ALBUMIN COMPLEXED WITH TETRADECANOIC ACID (MYRISTIC ACID) AND HEMIN===
-
==Overview==
+
<!--
-
BACKGROUND: Human serum albumin (HSA) is an abundant plasma protein that binds a wide variety of hydrophobic ligands including fatty acids, bilirubin, thyroxine and hemin. Although HSA-heme complexes do not bind oxygen reversibly, it may be possible to develop modified HSA proteins or heme groups that will confer this ability on the complex. RESULTS: We present here the crystal structure of a ternary HSA-hemin-myristate complex, formed at a 1:1:4 molar ratio, that contains a single hemin group bound to subdomain IB and myristate bound at six sites. The complex displays a conformation that is intermediate between defatted HSA and HSA-fatty acid complexes; this is likely to be due to low myristate occupancy in the fatty acid binding sites that drive the conformational change. The hemin group is bound within a narrow D-shaped hydrophobic cavity which usually accommodates fatty acid; the hemin propionate groups are coordinated by a triad of basic residues at the pocket entrance. The iron atom in the centre of the hemin is coordinated by Tyr161. CONCLUSION: The structure of the HSA-hemin-myristate complex (PDB ID 1o9x) reveals the key polar and hydrophobic interactions that determine the hemin-binding specificity of HSA. The details of the hemin-binding environment of HSA provide a structural foundation for efforts to modify the protein and/or the heme molecule in order to engineer complexes that have favourable oxygen-binding properties.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12846933}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12846933 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12846933}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Lipid-binding]]
[[Category: Lipid-binding]]
[[Category: Plasma protein]]
[[Category: Plasma protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:34:23 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:39:01 2008''

Revision as of 16:39, 27 July 2008

Image:1o9x.png

Template:STRUCTURE 1o9x

HUMAN SERUM ALBUMIN COMPLEXED WITH TETRADECANOIC ACID (MYRISTIC ACID) AND HEMIN

Template:ABSTRACT PUBMED 12846933

About this Structure

1O9X is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structural analysis of human serum albumin complexed with hemin and fatty acid., Zunszain PA, Ghuman J, Komatsu T, Tsuchida E, Curry S, BMC Struct Biol. 2003 Jul 7;3:6. Epub 2003 Jul 7. PMID:12846933

Page seeded by OCA on Sun Jul 27 19:39:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1o9x"
Personal tools