Pattern of cavities in globins: the case of human hemoglobin.
Our aim is to shed light on the conservation of potential ligand docking sites that play an important role in ligand dynamics of globins by using the technique of filling internal cavities naturally present in hemoglobin and myoglobin with xenon atoms. In particular, we present the high resolution s...
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Online Access: | https://hal.archives-ouvertes.fr/hal-01617675 https://doi.org/10.1002/bip.21201 |
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ftunivnantes:oai:HAL:hal-01617675v1 2023-05-15T18:26:49+02:00 Pattern of cavities in globins: the case of human hemoglobin. Savino, Carmelinda Miele, Adriana E Draghi, Federica Johnson, Kenneth A Sciara, Giuliano Brunori, Maurizio Vallone, Beatrice CNR, Inst Mol Biol & Pathol Università degli Studi di Roma "La Sapienza" = Sapienza University Rome (UNIROMA) Institut Pasteur, Fondation Cenci Bolognetti - Istituto Pasteur Italia, Fondazione Cenci Bolognetti Réseau International des Instituts Pasteur (RIIP) Italian MIUR FIRB2003 RBLA03133KC 004 2009 https://hal.archives-ouvertes.fr/hal-01617675 https://doi.org/10.1002/bip.21201 en eng HAL CCSD Wiley info:eu-repo/semantics/altIdentifier/doi/10.1002/bip.21201 info:eu-repo/semantics/altIdentifier/pmid/19365817 hal-01617675 https://hal.archives-ouvertes.fr/hal-01617675 doi:10.1002/bip.21201 PRODINRA: 405151 PUBMED: 19365817 WOS: 000270961600013 ISSN: 0006-3525 EISSN: 1097-0282 Biopolymers https://hal.archives-ouvertes.fr/hal-01617675 Biopolymers, 2009, 91 (12), pp.1097-1107. ⟨10.1002/bip.21201⟩ globin fold packing defects hydrophobic cavities structure-function relationship X-ray diffraction hemoglobinuria structure function relationship xrd wrapping cavite hydrophobe hémoglobine relation structure fonction diffraction x emballage [SDV]Life Sciences [q-bio] info:eu-repo/semantics/article Journal articles 2009 ftunivnantes https://doi.org/10.1002/bip.21201 2022-11-30T01:56:03Z Our aim is to shed light on the conservation of potential ligand docking sites that play an important role in ligand dynamics of globins by using the technique of filling internal cavities naturally present in hemoglobin and myoglobin with xenon atoms. In particular, we present the high resolution structures of the Xe-adduct of deoxygenated wild type human hemoglobin and a quadruple mutant (L(B10)Y and H(E7)Q in alpha and beta chains). For the sake of comparison we also determined under the same experimental conditions the xenon complex of wild type sperm whale myoglobin. The analysis revealed that the number and position of Xe binding cavities are different in the alpha and beta subunits, the latter being more similar to myoglobin. Notably, no proximal Xe docking site was detected in hemoglobin, at variance with myoglobin. The pattern of internal cavities accessibility and affinity for xenon suggests a different role for the dynamics of ligand migration in the two types of hemoglobin chains as compared to myoglobin. The number and position of hydrophobic cavities in hemoglobin are briefly discussed also in comparison with the data available for other members of the globin superfamily. Article in Journal/Newspaper Sperm whale Université de Nantes: HAL-UNIV-NANTES Biopolymers 91 12 1097 1107 |
institution |
Open Polar |
collection |
Université de Nantes: HAL-UNIV-NANTES |
op_collection_id |
ftunivnantes |
language |
English |
topic |
globin fold packing defects hydrophobic cavities structure-function relationship X-ray diffraction hemoglobinuria structure function relationship xrd wrapping cavite hydrophobe hémoglobine relation structure fonction diffraction x emballage [SDV]Life Sciences [q-bio] |
spellingShingle |
globin fold packing defects hydrophobic cavities structure-function relationship X-ray diffraction hemoglobinuria structure function relationship xrd wrapping cavite hydrophobe hémoglobine relation structure fonction diffraction x emballage [SDV]Life Sciences [q-bio] Savino, Carmelinda Miele, Adriana E Draghi, Federica Johnson, Kenneth A Sciara, Giuliano Brunori, Maurizio Vallone, Beatrice Pattern of cavities in globins: the case of human hemoglobin. |
topic_facet |
globin fold packing defects hydrophobic cavities structure-function relationship X-ray diffraction hemoglobinuria structure function relationship xrd wrapping cavite hydrophobe hémoglobine relation structure fonction diffraction x emballage [SDV]Life Sciences [q-bio] |
description |
Our aim is to shed light on the conservation of potential ligand docking sites that play an important role in ligand dynamics of globins by using the technique of filling internal cavities naturally present in hemoglobin and myoglobin with xenon atoms. In particular, we present the high resolution structures of the Xe-adduct of deoxygenated wild type human hemoglobin and a quadruple mutant (L(B10)Y and H(E7)Q in alpha and beta chains). For the sake of comparison we also determined under the same experimental conditions the xenon complex of wild type sperm whale myoglobin. The analysis revealed that the number and position of Xe binding cavities are different in the alpha and beta subunits, the latter being more similar to myoglobin. Notably, no proximal Xe docking site was detected in hemoglobin, at variance with myoglobin. The pattern of internal cavities accessibility and affinity for xenon suggests a different role for the dynamics of ligand migration in the two types of hemoglobin chains as compared to myoglobin. The number and position of hydrophobic cavities in hemoglobin are briefly discussed also in comparison with the data available for other members of the globin superfamily. |
author2 |
CNR, Inst Mol Biol & Pathol Università degli Studi di Roma "La Sapienza" = Sapienza University Rome (UNIROMA) Institut Pasteur, Fondation Cenci Bolognetti - Istituto Pasteur Italia, Fondazione Cenci Bolognetti Réseau International des Instituts Pasteur (RIIP) Italian MIUR FIRB2003 RBLA03133KC 004 |
format |
Article in Journal/Newspaper |
author |
Savino, Carmelinda Miele, Adriana E Draghi, Federica Johnson, Kenneth A Sciara, Giuliano Brunori, Maurizio Vallone, Beatrice |
author_facet |
Savino, Carmelinda Miele, Adriana E Draghi, Federica Johnson, Kenneth A Sciara, Giuliano Brunori, Maurizio Vallone, Beatrice |
author_sort |
Savino, Carmelinda |
title |
Pattern of cavities in globins: the case of human hemoglobin. |
title_short |
Pattern of cavities in globins: the case of human hemoglobin. |
title_full |
Pattern of cavities in globins: the case of human hemoglobin. |
title_fullStr |
Pattern of cavities in globins: the case of human hemoglobin. |
title_full_unstemmed |
Pattern of cavities in globins: the case of human hemoglobin. |
title_sort |
pattern of cavities in globins: the case of human hemoglobin. |
publisher |
HAL CCSD |
publishDate |
2009 |
url |
https://hal.archives-ouvertes.fr/hal-01617675 https://doi.org/10.1002/bip.21201 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
ISSN: 0006-3525 EISSN: 1097-0282 Biopolymers https://hal.archives-ouvertes.fr/hal-01617675 Biopolymers, 2009, 91 (12), pp.1097-1107. ⟨10.1002/bip.21201⟩ |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1002/bip.21201 info:eu-repo/semantics/altIdentifier/pmid/19365817 hal-01617675 https://hal.archives-ouvertes.fr/hal-01617675 doi:10.1002/bip.21201 PRODINRA: 405151 PUBMED: 19365817 WOS: 000270961600013 |
op_doi |
https://doi.org/10.1002/bip.21201 |
container_title |
Biopolymers |
container_volume |
91 |
container_issue |
12 |
container_start_page |
1097 |
op_container_end_page |
1107 |
_version_ |
1766208780885819392 |