2pmv
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(New page: 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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Revision as of 21:18, 12 November 2007
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Crystal Structure of Human Intrinsic Factor- Cobalamin Complex at 2.6 A Resolution
Contents |
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.
Disease
Known disease associated with this structure: Intrinsic factor deficiency OMIM:[609342]
About this Structure
2PMV is a Single protein structure of sequence from Homo sapiens with B12 as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of human intrinsic factor: Cobalamin complex at 2.6-A resolution., Mathews FS, Gordon MM, Chen Z, Rajashankar KR, Ealick SE, Alpers DH, Sukumar N, Proc Natl Acad Sci U S A. 2007 Oct 22;. PMID:17954916
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