Ololade fatunmbi
From Proteopedia
(Difference between revisions)
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<Structure load=‘4f4o’ size='350' frame='true' align='right' caption='hbhp’ scene='60/609783/Hbhpdimer/1' /> | <Structure load=‘4f4o’ size='350' frame='true' align='right' caption='hbhp’ scene='60/609783/Hbhpdimer/1' /> | ||
| - | Haptoglobin 1-1 (Hp), an abundant glycoprotein in blood binds free hemoglobin (Hb) dimers in one of the strongest non-covalent binding events known in biology. | + | Haptoglobin 1-1 (Hp), an abundant glycoprotein in blood binds free hemoglobin (Hb) dimers in one of the strongest non-covalent binding events known in biology. |
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== Function == | == Function == | ||
This interaction shields Hb residues that are prone to oxidative modification. | This interaction shields Hb residues that are prone to oxidative modification. | ||
== Disease == | == Disease == | ||
| - | Intravascular hemolysis | + | In red blood cells, Hb exists as a tetramer, composed of two Hb α1β1 dimers (Hbα1β1α2β2). When Hb is released from red blood cells it dissociates into dimers, exposing redox active residues. As mentioned before, Hp forms high affinity complexes with dissociated Hbα1β1 dimers released from red blood cells and shield these residues.Intravascular hemolysis |
== Relevance == | == Relevance == | ||
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== References == | == References == | ||
<references/> | <references/> | ||
| + | '''Ololade Fatunmbi'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
| + | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
Revision as of 23:19, 20 November 2014
Contents |
Haptoglobin-Hemoglobin Structure
|
Haptoglobin 1-1 (Hp), an abundant glycoprotein in blood binds free hemoglobin (Hb) dimers in one of the strongest non-covalent binding events known in biology.
Function
This interaction shields Hb residues that are prone to oxidative modification.
Disease
In red blood cells, Hb exists as a tetramer, composed of two Hb α1β1 dimers (Hbα1β1α2β2). When Hb is released from red blood cells it dissociates into dimers, exposing redox active residues. As mentioned before, Hp forms high affinity complexes with dissociated Hbα1β1 dimers released from red blood cells and shield these residues.Intravascular hemolysis
Relevance
Structural highlights
(http://www.umass.edu Igor)
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
</StructureSection>
References
Ololade Fatunmbi. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
