1ch4: Difference between revisions

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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="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1ch4, resolution 2.5Å" />

'''MODULE-SUBSTITUTED CHIMERA HEMOGLOBIN BETA-ALPHA (F133V)'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1CH4 OCA].

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==

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[[Category: respiratory protein]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on Thu ~~Nov 8~~ 12:59:~~03 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:00 2008''

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@@ Line 1: / Line 1: @@
-[[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="450" color="white" frame="true" align="right" spinBox="true"
 caption="1ch4, resolution 2.5&Aring;" />
 '''MODULE-SUBSTITUTED CHIMERA HEMOGLOBIN BETA-ALPHA (F133V)'''<br />
 ==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.
+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==
-CH4 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CH4 OCA].
+CH4 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==
@@ Line 27: / Line 26: @@
 [[Category: respiratory protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov  8 12:59:03 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:00 2008''