6ii1: Difference between revisions
m Protected "6ii1" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
The | ==Crystal Structure Analysis of CO form hemoglobin from Bos taurus== | ||
<StructureSection load='6ii1' size='340' side='right' caption='[[6ii1]], [[Resolution|resolution]] 1.34Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ii1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6II1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6II1 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ii1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ii1 OCA], [http://pdbe.org/6ii1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ii1 RCSB], [http://www.ebi.ac.uk/pdbsum/6ii1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ii1 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/HBA_BOVIN HBA_BOVIN]] Involved in oxygen transport from the lung to the various peripheral tissues. [[http://www.uniprot.org/uniprot/HBB_BOVIN HBB_BOVIN]] Involved in oxygen transport from the lung to the various peripheral tissues. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A core-shell ensemble of bovine hemoglobin (Hb) and human serum albumin (HSA) is an artificial O2 carrier as a red blood cell substitute. This protein particle is created by covalent wrapping of a carbonyl Hb with HSAs: HbR-HSA3 cluster, where HbR signifies the use of carbonyl Hb [relaxed(R)-state conformation] as a starting material. The HbR-HSA3 cluster exhibits high O2 affinity and low cooperativity. Analysis of the quaternary structure of the central HbR in the cluster revealed that its high O2 affinity is attributed to the physically immobile HbR nucleus. Circular dichroism and UV-vis absorption spectroscopy showed that the structure of deoxy HbR core closely resembles the R-state. The crystal structure of Lys-modified carbonyl HbR was superimposed to that of carbonyl Hb. These results imply that chemical modifications of the surface Lys groups and Cys-93(beta) of the carbonyl Hb with crosslinking agent interfered in the quaternary structure movement from the R-state to Tense(T)-state. As expected, coupling of deoxy Hb (T-state) with HSAs yielded HbT-HSA3 cluster having low O2 affinity. The mixing of HbR-HSA3 and HbT-HSA3 clusters conferred a tailor-made formulation of artificial O2 carrier with a desired O2 affinity (P50). | |||
Quaternary Structure Analysis of a Hemoglobin Core in Hemoglobin-Albumin Cluster.,Morita Y, Yamada T, Kureishi M, Kihira K, Komatsu T J Phys Chem B. 2018 Nov 16. doi: 10.1021/acs.jpcb.8b10077. PMID:30444368<ref>PMID:30444368</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6ii1" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bos taurus]] | |||
[[Category: Kihira, K]] | |||
[[Category: Komatsu, T]] | [[Category: Komatsu, T]] | ||
[[Category: Kureishi, M]] | [[Category: Kureishi, M]] | ||
[[Category: Morita, Y]] | |||
[[Category: Yamada, T]] | [[Category: Yamada, T]] | ||
[[Category: Globin family]] | |||
[[Category: Heme binding]] | |||
[[Category: Iron ion binding]] | |||
[[Category: Oxygen transport]] | |||
[[Category: Red blood cell]] | |||
Revision as of 09:55, 12 December 2018
Crystal Structure Analysis of CO form hemoglobin from Bos taurusCrystal Structure Analysis of CO form hemoglobin from Bos taurus
Structural highlights
Function[HBA_BOVIN] Involved in oxygen transport from the lung to the various peripheral tissues. [HBB_BOVIN] Involved in oxygen transport from the lung to the various peripheral tissues. Publication Abstract from PubMedA core-shell ensemble of bovine hemoglobin (Hb) and human serum albumin (HSA) is an artificial O2 carrier as a red blood cell substitute. This protein particle is created by covalent wrapping of a carbonyl Hb with HSAs: HbR-HSA3 cluster, where HbR signifies the use of carbonyl Hb [relaxed(R)-state conformation] as a starting material. The HbR-HSA3 cluster exhibits high O2 affinity and low cooperativity. Analysis of the quaternary structure of the central HbR in the cluster revealed that its high O2 affinity is attributed to the physically immobile HbR nucleus. Circular dichroism and UV-vis absorption spectroscopy showed that the structure of deoxy HbR core closely resembles the R-state. The crystal structure of Lys-modified carbonyl HbR was superimposed to that of carbonyl Hb. These results imply that chemical modifications of the surface Lys groups and Cys-93(beta) of the carbonyl Hb with crosslinking agent interfered in the quaternary structure movement from the R-state to Tense(T)-state. As expected, coupling of deoxy Hb (T-state) with HSAs yielded HbT-HSA3 cluster having low O2 affinity. The mixing of HbR-HSA3 and HbT-HSA3 clusters conferred a tailor-made formulation of artificial O2 carrier with a desired O2 affinity (P50). Quaternary Structure Analysis of a Hemoglobin Core in Hemoglobin-Albumin Cluster.,Morita Y, Yamada T, Kureishi M, Kihira K, Komatsu T J Phys Chem B. 2018 Nov 16. doi: 10.1021/acs.jpcb.8b10077. PMID:30444368[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||