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2pmv
From Proteopedia
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|PDB= 2pmv |SIZE=350|CAPTION= <scene name='initialview01'>2pmv</scene>, resolution 2.60Å | |PDB= 2pmv |SIZE=350|CAPTION= <scene name='initialview01'>2pmv</scene>, resolution 2.60Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=B12:COBALAMIN'>B12</scene> | + | |LIGAND= <scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pmv OCA], [http://www.ebi.ac.uk/pdbsum/2pmv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2pmv RCSB]</span> | ||
}} | }} | ||
| Line 14: | Line 17: | ||
==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. | ||
| - | |||
| - | ==Disease== | ||
| - | 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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[[Category: Rajashankar, K R.]] | [[Category: Rajashankar, K R.]] | ||
[[Category: Sukumar, N.]] | [[Category: Sukumar, N.]] | ||
| - | [[Category: B12]] | ||
[[Category: cobalamin transport protein alpha6-alpha6 motif two domain protein]] | [[Category: cobalamin transport protein alpha6-alpha6 motif two domain protein]] | ||
[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:38:08 2008'' |
Revision as of 01:38, 31 March 2008
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| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Human Intrinsic Factor- Cobalamin Complex at 2.6 A Resolution
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.
About this Structure
2PMV is a Single protein structure of sequence from Homo sapiens. 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
Page seeded by OCA on Mon Mar 31 04:38:08 2008
