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.


1hbr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1hbr.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1hbr.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hbr| PDB=1hbr | SCENE= }}
{{STRUCTURE_1hbr| PDB=1hbr | SCENE= }}
-
'''R-STATE FORM OF CHICKEN HEMOGLOBIN D'''
+
===R-STATE FORM OF CHICKEN HEMOGLOBIN D===
-
==Overview==
+
<!--
-
Oxygen binding by chicken blood shows enhanced cooperativity at high levels of oxygen saturation. This implies that deoxy hemoglobin tetramers self-associate. The crystal structure of an R-state form of chicken hemoglobin D has been solved to 2.3-A resolution using molecular replacement phases derived from human oxyhemoglobin. The model consists of an alpha2 beta2 tetramer in the asymmetric unit and has been refined to a R-factor of 0.222 (R-free = 0.257) for 29,702 reflections between 10.0- and 2.3-A resolution. Chicken Hb D differs most from human oxyhemoglobin in the AB and GH corners of the alpha subunits and the EF corner of the beta subunits. Reanalysis of published oxygen binding data for chicken Hbs shows that both chicken Hb A and Hb D possess enhanced cooperativity in vitro when inositol hexaphosphate is present. The electrostatic surface potential for a calculated model of chicken deoxy-Hb D tetramers shows a pronounced hydrophobic patch that involves parts of the D and E helices of the beta subunits. This hydrophobic patch is a promising candidate for a tetramer-tetramer interface that could regulate oxygen binding via the distal histidine.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10037733}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10037733 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10037733}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: High cooperatiity]]
[[Category: High cooperatiity]]
[[Category: Oxygen transport]]
[[Category: Oxygen transport]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:40:28 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 07:57:18 2008''

Revision as of 04:57, 1 July 2008

Image:1hbr.png

Template:STRUCTURE 1hbr

R-STATE FORM OF CHICKEN HEMOGLOBIN D

Template:ABSTRACT PUBMED 10037733

About this Structure

1HBR is a Protein complex structure of sequences from Gallus gallus. Full crystallographic information is available from OCA.

Reference

The structural and functional analysis of the hemoglobin D component from chicken., Knapp JE, Oliveira MA, Xie Q, Ernst SR, Riggs AF, Hackert ML, J Biol Chem. 1999 Mar 5;274(10):6411-20. PMID:10037733

Page seeded by OCA on Tue Jul 1 07:57:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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