Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 141-150 |
| Number of pages | 10 |
| Journal | The Protein Journal |
| Volume | 27 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Apr 2008 |
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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 journal › Article
TY - JOUR
T1 - Low oxygen affinity in reptilian hemoglobin D
T2 - prediction of residue interactions in Geochelone carbonaria HbD by homology modeling
AU - Lutfullah, Ghosia
AU - Khalil, Hilal S.
AU - Amin, Farha
AU - Azhar, Noreen
PY - 2008/4
Y1 - 2008/4
N2 - 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.
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.
U2 - 10.1007/s10930-007-9117-9
DO - 10.1007/s10930-007-9117-9
M3 - Article
VL - 27
SP - 141
EP - 150
JO - Protein Journal
JF - Protein Journal
SN - 1572-3887
IS - 3
ER -