2pmv: Difference between revisions
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New page: left|200px<br /> <applet load="2pmv" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pmv, resolution 2.60Å" /> '''Crystal Structure o... |
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[[Image:2pmv.gif|left|200px]]<br /> | [[Image:2pmv.gif|left|200px]]<br /><applet load="2pmv" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="2pmv" size=" | |||
caption="2pmv, resolution 2.60Å" /> | caption="2pmv, resolution 2.60Å" /> | ||
'''Crystal Structure of Human Intrinsic Factor- Cobalamin Complex at 2.6 A Resolution'''<br /> | '''Crystal Structure of Human Intrinsic Factor- Cobalamin Complex at 2.6 A Resolution'''<br /> | ||
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==Overview== | ==Overview== | ||
The structure of intrinsic factor (IF) in complex with cobalamin (Cbl) was, determined at 2.6-A resolution. The overall fold of the molecule is that, of an alpha(6)/alpha(6) barrel. It is a two-domain protein, and the Cbl is, bound at the interface of the domains in a base-on conformation., Surprisingly, two full-length molecules, each comprising an alpha- and a, beta-domain and one Cbl, and two truncated molecules with only an alpha-, domain are present in the same asymmetric unit. The environment around Cbl, is dominated by uncharged residues, and the sixth coordinate position of, Co(2+) is empty. A detailed comparison between the IF-B12 complex and, another Cbl transport protein complex, trans-Cbl-B12, has been made. The, pH effect on the binding of Cbl analogues in transport proteins is, analyzed. A possible basis for the lack of interchangeability of human and, rat IF receptors is presented. | The structure of intrinsic factor (IF) in complex with cobalamin (Cbl) was, determined at 2.6-A resolution. The overall fold of the molecule is that, of an alpha(6)/alpha(6) barrel. It is a two-domain protein, and the Cbl is, bound at the interface of the domains in a base-on conformation., Surprisingly, two full-length molecules, each comprising an alpha- and a, beta-domain and one Cbl, and two truncated molecules with only an alpha-, domain are present in the same asymmetric unit. The environment around Cbl, is dominated by uncharged residues, and the sixth coordinate position of, Co(2+) is empty. A detailed comparison between the IF-B12 complex and, another Cbl transport protein complex, trans-Cbl-B12, has been made. The, pH effect on the binding of Cbl analogues in transport proteins is, analyzed. A possible basis for the lack of interchangeability of human and, rat IF receptors is presented. | ||
==About this Structure== | ==About this Structure== | ||
2PMV 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 B12 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 2PMV 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=B12:'>B12</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PMV OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transport protein]] | [[Category: transport protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:19:52 2008'' | ||
