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.


1g09

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1g09.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1g09.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1g09| PDB=1g09 | SCENE= }}
{{STRUCTURE_1g09| PDB=1g09 | SCENE= }}
-
'''CARBONMONOXY LIGANDED BOVINE HEMOGLOBIN PH 7.2'''
+
===CARBONMONOXY LIGANDED BOVINE HEMOGLOBIN PH 7.2===
-
==Overview==
+
<!--
-
Initial crystallographic studies suggested that fully liganded mammalian hemoglobin can adopt only a single quaternary structure, the quaternary R structure. However, more recent crystallographic studies revealed the existence of a second quaternary structure for liganded hemoglobin, the quaternary R2 structure. Since these quaternary structures can be crystallized, both must be energetically accessible structures that coexist in solution. Unanswered questions include (i) the relative abundance of the R and R2 structures under various solution conditions and (ii) whether other quaternary structures are energetically accessible for the liganded alpha(2)beta(2) hemoglobin tetramer. Although crystallographic methods cannot directly answer the first question, they represent the most direct and most accurate approach to answering the second question. We now have determined and refined three different crystal structures of bovine carbonmonoxyhemoglobin. These structures provide clear evidence that the dimer-dimer interface of liganded hemoglobin has a wide range of energetically accessible structures that are related to each other by a simple sliding motion. The dimer-dimer interface acts as a "molecular slide bearing" that allows the two alpha beta dimers to slide back and forth without greatly altering the number or the nature of the intersubunit contacts. Since the general stereochemical features of this interface are not unusual, it is likely that interface sliding of the kind displayed by fully liganded hemoglobin plays important structural and functional roles in many other protein assemblies.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11112521}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11112521 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11112521}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Liganded]]
[[Category: Liganded]]
[[Category: Protoporphyrin ix]]
[[Category: Protoporphyrin ix]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:58:07 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:12:33 2008''

Revision as of 01:12, 1 July 2008

Image:1g09.png

Template:STRUCTURE 1g09

CARBONMONOXY LIGANDED BOVINE HEMOGLOBIN PH 7.2

Template:ABSTRACT PUBMED 11112521

About this Structure

1G09 is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

Reference

Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin., Mueser TC, Rogers PH, Arnone A, Biochemistry. 2000 Dec 19;39(50):15353-64. PMID:11112521

Page seeded by OCA on Tue Jul 1 04:12:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1g09"
Personal tools