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| {{STRUCTURE_1c40| PDB=1c40 | SCENE= }} | | {{STRUCTURE_1c40| PDB=1c40 | SCENE= }} |
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| '''BAR-HEADED GOOSE HEMOGLOBIN (AQUOMET FORM)'''
| | ===BAR-HEADED GOOSE HEMOGLOBIN (AQUOMET FORM)=== |
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| ==Overview==
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| Haemoglobin from the bar-headed goose (Anser indicus) has higher oxygen affinity than that from its lowland relatives such as greylag goose (A. anser). The crystal structure of bar-headed goose aquomet haemoglobin was determined at 2.3 A resolution and compared with the structures of the goose oxy, human, horse and other avian haemoglobins and the sequences of other avian haemoglobins. Four amino-acid residues differ between greylag goose and bar-headed goose haemoglobins, among which Alaalpha119 and Aspbeta125 in bar-headed goose haemoglobin reduces the contacts between the alpha(1) and beta(1) subunits compared with Pro and Glu, respectively, and therefore may increase the oxygen affinity by loosening the alpha(1)beta(1) interface. Compared with human oxy haemoglobin, the relative orientation of two alphabeta dimers in the bar-headed goose aquomet and oxy Hbs are rotated by about 4 degrees, indicating a unique quaternary structural difference from the typical R state. This new 'R(H)' state is probably correlated with the higher oxygen affinity of bar-headed goose haemoglobin.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11375496}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11375496 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11375496}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Oxygen transport]] | | [[Category: Oxygen transport]] |
| [[Category: Respiratory protein]] | | [[Category: Respiratory protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:18:17 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:10:53 2008'' |
