Low oxygen affinity in reptilian hemoglobin D: prediction of residue interactions in Geochelone carbonaria HbD by homology modeling

Ghosia Lutfullah, Hilal S. Khalil, Farha Amin, Noreen Azhar

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

The homology model of hemoglobin D from Geochelone carbonaria, the red-footed tortoise was predicted using the 3D structure coordinates of Geochelone gigantea hemoglobin D as the template. The model was built using the program, MODELLER (8v1) and evaluated with PROCHECK and PROSA. The present study features an in-depth analysis of the 3D model and its conformational changes brought about with variations in its environment. These structural changes are correlated with its ability to adapt to different environmental constraints enabling the organism to better suit to its natural habitat. The model shows additional contacts between amino acid pairs of α-119 and β-55, α-35 and β-124, α-103 and β-112, α-115 and β-116, α-120 and β-52, α-120 and β-55, α-36 and β-127 which are not found in human hemoglobin. It is predicted that these contacts may result in T-state stabilization thus lowering oxygen affinity. Furthermore, decrease in the interaction of phosphate heteroatoms with the amino acid residues of G. carbonaria Hb was also predicted in this study.
Original languageEnglish
Pages (from-to)141-150
Number of pages10
JournalThe Protein Journal
Volume27
Issue number3
DOIs
Publication statusPublished - Apr 2008

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Hemoglobin
Oxygen
Amino Acids
Turtles
Ecosystem
Amino acids
Hemoglobins
Phosphates
Stabilization
hemoglobin D

Cite this

Lutfullah, Ghosia ; Khalil, Hilal S. ; Amin, Farha ; Azhar, Noreen. / Low oxygen affinity in reptilian hemoglobin D : prediction of residue interactions in Geochelone carbonaria HbD by homology modeling. In: The Protein Journal. 2008 ; Vol. 27, No. 3. pp. 141-150.
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abstract = "The homology model of hemoglobin D from Geochelone carbonaria, the red-footed tortoise was predicted using the 3D structure coordinates of Geochelone gigantea hemoglobin D as the template. The model was built using the program, MODELLER (8v1) and evaluated with PROCHECK and PROSA. The present study features an in-depth analysis of the 3D model and its conformational changes brought about with variations in its environment. These structural changes are correlated with its ability to adapt to different environmental constraints enabling the organism to better suit to its natural habitat. The model shows additional contacts between amino acid pairs of α-119 and β-55, α-35 and β-124, α-103 and β-112, α-115 and β-116, α-120 and β-52, α-120 and β-55, α-36 and β-127 which are not found in human hemoglobin. It is predicted that these contacts may result in T-state stabilization thus lowering oxygen affinity. Furthermore, decrease in the interaction of phosphate heteroatoms with the amino acid residues of G. carbonaria Hb was also predicted in this study.",
author = "Ghosia Lutfullah and Khalil, {Hilal S.} and Farha Amin and Noreen Azhar",
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Low oxygen affinity in reptilian hemoglobin D : prediction of residue interactions in Geochelone carbonaria HbD by homology modeling. / Lutfullah, Ghosia; Khalil, Hilal S.; Amin, Farha; Azhar, Noreen.

In: The Protein Journal, Vol. 27, No. 3, 04.2008, p. 141-150.

Research output: Contribution to journalArticle

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AB - The homology model of hemoglobin D from Geochelone carbonaria, the red-footed tortoise was predicted using the 3D structure coordinates of Geochelone gigantea hemoglobin D as the template. The model was built using the program, MODELLER (8v1) and evaluated with PROCHECK and PROSA. The present study features an in-depth analysis of the 3D model and its conformational changes brought about with variations in its environment. These structural changes are correlated with its ability to adapt to different environmental constraints enabling the organism to better suit to its natural habitat. The model shows additional contacts between amino acid pairs of α-119 and β-55, α-35 and β-124, α-103 and β-112, α-115 and β-116, α-120 and β-52, α-120 and β-55, α-36 and β-127 which are not found in human hemoglobin. It is predicted that these contacts may result in T-state stabilization thus lowering oxygen affinity. Furthermore, decrease in the interaction of phosphate heteroatoms with the amino acid residues of G. carbonaria Hb was also predicted in this study.

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