2pgh
From Proteopedia
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| - | [[Image:2pgh.jpg|left|200px]] | + | [[Image:2pgh.jpg|left|200px]] |
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| - | '''STRUCTURE DETERMINATION OF AQUOMET PORCINE HEMOGLOBIN AT 2.8 ANGSTROM RESOLUTION''' | + | {{Structure |
| + | |PDB= 2pgh |SIZE=350|CAPTION= <scene name='initialview01'>2pgh</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE DETERMINATION OF AQUOMET PORCINE HEMOGLOBIN AT 2.8 ANGSTROM RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2PGH is a [ | + | 2PGH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. This structure supersedes the now removed PDB entry 1PGH. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PGH OCA]. |
==Reference== | ==Reference== | ||
| - | Structure determination of aquomet porcine hemoglobin at 2.8 A resolution., Katz DS, White SP, Huang W, Kumar R, Christianson DW, J Mol Biol. 1994 Dec 16;244(5):541-53. PMID:[http:// | + | Structure determination of aquomet porcine hemoglobin at 2.8 A resolution., Katz DS, White SP, Huang W, Kumar R, Christianson DW, J Mol Biol. 1994 Dec 16;244(5):541-53. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7990139 7990139] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
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[[Category: oxygen transport]] | [[Category: oxygen transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:12:46 2008'' |
Revision as of 16:12, 20 March 2008
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| , resolution 2.8Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE DETERMINATION OF AQUOMET PORCINE HEMOGLOBIN AT 2.8 ANGSTROM RESOLUTION
Overview
Considerable attention is currently focused on hemoglobins from lower mammals, such as the pig, for potential use in cell-free blood substitute preparations safe for use in humans. As the first step in the elucidation of structure-function relationships in porcine hemoglobin, we have determined the three-dimensional structure of aquomet porcine hemoglobin at 2.8 A resolution. Overall, the porcine hemoglobin tetramer is structurally similar to that of human oxyhemoglobin, and the r.m.s. deviation of all backbone atoms (minus five residues at the amino and carboxyl termini of each subunit) is 0.8 A. This similarity is not unexpected given that human and porcine hemoglobins exhibit 85% sequence identity. However, regions of subtle structural differences are implicated in subtle functional differences between the two proteins, such as the 20 to 25% inhibition of the alkaline Bohr effect and the accompanying reduction in oxygen-linked chloride binding observed for porcine hemoglobin. The structural similarity of these two mammalian hemoglobins also rationalizes the novel hybridization behavior of pig and human subunits in transgenic pigs expressing both porcine and human hemoglobins in porcine erythrocytes.
About this Structure
2PGH is a Protein complex structure of sequences from Sus scrofa. This structure supersedes the now removed PDB entry 1PGH. Full crystallographic information is available from OCA.
Reference
Structure determination of aquomet porcine hemoglobin at 2.8 A resolution., Katz DS, White SP, Huang W, Kumar R, Christianson DW, J Mol Biol. 1994 Dec 16;244(5):541-53. PMID:7990139
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