1ch4
From Proteopedia
(New page: 200px<br /> <applet load="1ch4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ch4, resolution 2.5Å" /> '''MODULE-SUBSTITUTED C...) |
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| - | [[Image:1ch4.gif|left|200px]]<br /> | + | [[Image:1ch4.gif|left|200px]]<br /><applet load="1ch4" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ch4" size=" | + | |
caption="1ch4, resolution 2.5Å" /> | caption="1ch4, resolution 2.5Å" /> | ||
'''MODULE-SUBSTITUTED CHIMERA HEMOGLOBIN BETA-ALPHA (F133V)'''<br /> | '''MODULE-SUBSTITUTED CHIMERA HEMOGLOBIN BETA-ALPHA (F133V)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the homotetramer of a chimera beta alpha-subunit | + | The crystal structure of the homotetramer of a chimera beta alpha-subunit of human hemoglobin was refined at 2.5 A resolution. The chimera subunit was constructed by replacing an exon-encoded module M4 of the beta-subunit with that of the alpha-subunit, simulating an exon-shuffling event. The implanted module M4 retained the native alpha-subunit structure, while module M3 was disturbed around the site where a new type of intron was recently found. Some of the residues were found in alternative conformations that avoid steric hindrance at the subunit interface. The modules are modestly rigid in their backbone structures by using side-chains to compensate for interface incompatibility. |
==About this Structure== | ==About this Structure== | ||
| - | 1CH4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with HEM and CMO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1CH4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=CMO:'>CMO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CH4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: respiratory protein]] | [[Category: respiratory protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:00 2008'' |
Revision as of 10:06, 21 February 2008
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MODULE-SUBSTITUTED CHIMERA HEMOGLOBIN BETA-ALPHA (F133V)
Overview
The crystal structure of the homotetramer of a chimera beta alpha-subunit of human hemoglobin was refined at 2.5 A resolution. The chimera subunit was constructed by replacing an exon-encoded module M4 of the beta-subunit with that of the alpha-subunit, simulating an exon-shuffling event. The implanted module M4 retained the native alpha-subunit structure, while module M3 was disturbed around the site where a new type of intron was recently found. Some of the residues were found in alternative conformations that avoid steric hindrance at the subunit interface. The modules are modestly rigid in their backbone structures by using side-chains to compensate for interface incompatibility.
About this Structure
1CH4 is a Protein complex structure of sequences from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of a protein with an artificial exon-shuffling, module M4-substituted chimera hemoglobin beta alpha, at 2.5 A resolution., Shirai T, Fujikake M, Yamane T, Inaba K, Ishimori K, Morishima I, J Mol Biol. 1999 Mar 26;287(2):369-82. PMID:10080899
Page seeded by OCA on Thu Feb 21 12:06:00 2008
Categories: Homo sapiens | Protein complex | Fujikake, M. | Inaba, K. | Ishimori, K. | Morishima, I. | Shirai, T. | Yamane, T. | CMO | HEM | Chimera protein | Heme | Oxygen transport | Respiratory protein
