2pmv

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==Overview==
==Overview==
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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.
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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.
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==Disease==
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Known disease associated with this structure: Intrinsic factor deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=609342 609342]]
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17954916 17954916]
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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 30;104(44):17311-6. Epub 2007 Oct 22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17954916 17954916]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Alpers, D.H.]]
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[[Category: Alpers, D H.]]
[[Category: Chen, Z.]]
[[Category: Chen, Z.]]
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[[Category: Ealick, S.E.]]
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[[Category: Ealick, S E.]]
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[[Category: Gordon, M.M.]]
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[[Category: Gordon, M M.]]
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[[Category: Mathews, F.S.]]
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[[Category: Mathews, F S.]]
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[[Category: Rajashankar, K.R.]]
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[[Category: Rajashankar, K R.]]
[[Category: Sukumar, N.]]
[[Category: Sukumar, N.]]
[[Category: B12]]
[[Category: B12]]
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[[Category: transport protein]]
[[Category: transport protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:19:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:31:07 2008''

Revision as of 16:31, 21 February 2008


2pmv, resolution 2.60Å

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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 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 30;104(44):17311-6. Epub 2007 Oct 22. PMID:17954916

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