1n5u: Difference between revisions

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New page: left|200px<br /> <applet load="1n5u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n5u, resolution 1.90Å" /> '''X-RAY STUDY OF HUMA...
 
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[[Image:1n5u.gif|left|200px]]<br />
[[Image:1n5u.gif|left|200px]]<br /><applet load="1n5u" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1n5u" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1n5u, resolution 1.90&Aring;" />
caption="1n5u, resolution 1.90&Aring;" />
'''X-RAY STUDY OF HUMAN SERUM ALBUMIN COMPLEXED WITH HEME'''<br />
'''X-RAY STUDY OF HUMAN SERUM ALBUMIN COMPLEXED WITH HEME'''<br />


==Overview==
==Overview==
The high resolution structure of hemalbumin was determined by single, crystal X-ray diffraction to a resolution of 1.9 A. The structure revealed, the protoporphyrin IX bound to a single site within a hydrophobic cavity, in subdomain IB, one of the principal binding sites for long chain fatty, acid. The iron is penta coordinated with the fifth ligand comprised of the, hydroxyl oxygen of Tyr-161 (phenolic oxygen to heme plane distance: 2.73, A) in an otherwise completely hydrophobic pocket. The heme propionic acid, residues form salt bridges with His-142 and Lys-190, which together with a, series of hydrophobic interactions, enclose and secure the heme within the, IB helical motif. A detailed discussion of the structure together with its, implications for the development of potential blood substitutes is, presented.
The high resolution structure of hemalbumin was determined by single crystal X-ray diffraction to a resolution of 1.9 A. The structure revealed the protoporphyrin IX bound to a single site within a hydrophobic cavity in subdomain IB, one of the principal binding sites for long chain fatty acid. The iron is penta coordinated with the fifth ligand comprised of the hydroxyl oxygen of Tyr-161 (phenolic oxygen to heme plane distance: 2.73 A) in an otherwise completely hydrophobic pocket. The heme propionic acid residues form salt bridges with His-142 and Lys-190, which together with a series of hydrophobic interactions, enclose and secure the heme within the IB helical motif. A detailed discussion of the structure together with its implications for the development of potential blood substitutes is presented.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1N5U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MYR and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N5U OCA].  
1N5U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MYR:'>MYR</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N5U OCA].  


==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Carter, D.C.]]
[[Category: Carter, D C.]]
[[Category: Ho, J.X.]]
[[Category: Ho, J X.]]
[[Category: Robert, J.]]
[[Category: Robert, J.]]
[[Category: Ruble, J.]]
[[Category: Ruble, J.]]
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[[Category: plasma protein]]
[[Category: plasma protein]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:17:57 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:32 2008''

Revision as of 15:02, 21 February 2008

File:1n5u.gif


1n5u, resolution 1.90Å

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X-RAY STUDY OF HUMAN SERUM ALBUMIN COMPLEXED WITH HEME

OverviewOverview

The high resolution structure of hemalbumin was determined by single crystal X-ray diffraction to a resolution of 1.9 A. The structure revealed the protoporphyrin IX bound to a single site within a hydrophobic cavity in subdomain IB, one of the principal binding sites for long chain fatty acid. The iron is penta coordinated with the fifth ligand comprised of the hydroxyl oxygen of Tyr-161 (phenolic oxygen to heme plane distance: 2.73 A) in an otherwise completely hydrophobic pocket. The heme propionic acid residues form salt bridges with His-142 and Lys-190, which together with a series of hydrophobic interactions, enclose and secure the heme within the IB helical motif. A detailed discussion of the structure together with its implications for the development of potential blood substitutes is presented.

DiseaseDisease

Known diseases associated with this structure: Analbuminemia OMIM:[103600], Dysalbuminemic hyperthyroxinemia OMIM:[103600], Dysalbuminemic hyperzincemia OMIM:[103600]

About this StructureAbout this Structure

1N5U is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

The atomic structure of human methemalbumin at 1.9 A., Wardell M, Wang Z, Ho JX, Robert J, Ruker F, Ruble J, Carter DC, Biochem Biophys Res Commun. 2002 Mar 8;291(4):813-9. PMID:11866438

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