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[[Image:1hbr.jpg|left|200px]]
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{{STRUCTURE_1hbr|  PDB=1hbr  |  SCENE=  }}
'''R-STATE FORM OF CHICKEN HEMOGLOBIN D'''


==R-STATE FORM OF CHICKEN HEMOGLOBIN D==
<StructureSection load='1hbr' size='340' side='right'caption='[[1hbr]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hbr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HBR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HBR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=1hbr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hbr OCA], [https://pdbe.org/1hbr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hbr RCSB], [https://www.ebi.ac.uk/pdbsum/1hbr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hbr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HBAD_CHICK HBAD_CHICK] Involved in oxygen transport from the lung to the various peripheral tissues.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hb/1hbr_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hbr ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Oxygen binding by chicken blood shows enhanced cooperativity at high levels of oxygen saturation. This implies that deoxy hemoglobin tetramers self-associate. The crystal structure of an R-state form of chicken hemoglobin D has been solved to 2.3-A resolution using molecular replacement phases derived from human oxyhemoglobin. The model consists of an alpha2 beta2 tetramer in the asymmetric unit and has been refined to a R-factor of 0.222 (R-free = 0.257) for 29,702 reflections between 10.0- and 2.3-A resolution. Chicken Hb D differs most from human oxyhemoglobin in the AB and GH corners of the alpha subunits and the EF corner of the beta subunits. Reanalysis of published oxygen binding data for chicken Hbs shows that both chicken Hb A and Hb D possess enhanced cooperativity in vitro when inositol hexaphosphate is present. The electrostatic surface potential for a calculated model of chicken deoxy-Hb D tetramers shows a pronounced hydrophobic patch that involves parts of the D and E helices of the beta subunits. This hydrophobic patch is a promising candidate for a tetramer-tetramer interface that could regulate oxygen binding via the distal histidine.


==Overview==
The structural and functional analysis of the hemoglobin D component from chicken.,Knapp JE, Oliveira MA, Xie Q, Ernst SR, Riggs AF, Hackert ML J Biol Chem. 1999 Mar 5;274(10):6411-20. PMID:10037733<ref>PMID:10037733</ref>
Oxygen binding by chicken blood shows enhanced cooperativity at high levels of oxygen saturation. This implies that deoxy hemoglobin tetramers self-associate. The crystal structure of an R-state form of chicken hemoglobin D has been solved to 2.3-A resolution using molecular replacement phases derived from human oxyhemoglobin. The model consists of an alpha2 beta2 tetramer in the asymmetric unit and has been refined to a R-factor of 0.222 (R-free = 0.257) for 29,702 reflections between 10.0- and 2.3-A resolution. Chicken Hb D differs most from human oxyhemoglobin in the AB and GH corners of the alpha subunits and the EF corner of the beta subunits. Reanalysis of published oxygen binding data for chicken Hbs shows that both chicken Hb A and Hb D possess enhanced cooperativity in vitro when inositol hexaphosphate is present. The electrostatic surface potential for a calculated model of chicken deoxy-Hb D tetramers shows a pronounced hydrophobic patch that involves parts of the D and E helices of the beta subunits. This hydrophobic patch is a promising candidate for a tetramer-tetramer interface that could regulate oxygen binding via the distal histidine.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1HBR is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HBR OCA].
</div>
<div class="pdbe-citations 1hbr" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
The structural and functional analysis of the hemoglobin D component from chicken., Knapp JE, Oliveira MA, Xie Q, Ernst SR, Riggs AF, Hackert ML, J Biol Chem. 1999 Mar 5;274(10):6411-20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10037733 10037733]
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Ernst, S R.]]
[[Category: Ernst SR]]
[[Category: Hackert, M L.]]
[[Category: Hackert ML]]
[[Category: Knapp, E.]]
[[Category: Knapp E]]
[[Category: Oliveira, M A.]]
[[Category: Oliveira MA]]
[[Category: Riggs, A F.]]
[[Category: Riggs AF]]
[[Category: Xie, Q.]]
[[Category: Xie Q]]
[[Category: Avian]]
[[Category: Hemoglobin]]
[[Category: High cooperatiity]]
[[Category: Oxygen transport]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:40:28 2008''

Latest revision as of 09:12, 9 August 2023

R-STATE FORM OF CHICKEN HEMOGLOBIN DR-STATE FORM OF CHICKEN HEMOGLOBIN D

Structural highlights

1hbr is a 4 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HBAD_CHICK Involved in oxygen transport from the lung to the various peripheral tissues.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Oxygen binding by chicken blood shows enhanced cooperativity at high levels of oxygen saturation. This implies that deoxy hemoglobin tetramers self-associate. The crystal structure of an R-state form of chicken hemoglobin D has been solved to 2.3-A resolution using molecular replacement phases derived from human oxyhemoglobin. The model consists of an alpha2 beta2 tetramer in the asymmetric unit and has been refined to a R-factor of 0.222 (R-free = 0.257) for 29,702 reflections between 10.0- and 2.3-A resolution. Chicken Hb D differs most from human oxyhemoglobin in the AB and GH corners of the alpha subunits and the EF corner of the beta subunits. Reanalysis of published oxygen binding data for chicken Hbs shows that both chicken Hb A and Hb D possess enhanced cooperativity in vitro when inositol hexaphosphate is present. The electrostatic surface potential for a calculated model of chicken deoxy-Hb D tetramers shows a pronounced hydrophobic patch that involves parts of the D and E helices of the beta subunits. This hydrophobic patch is a promising candidate for a tetramer-tetramer interface that could regulate oxygen binding via the distal histidine.

The structural and functional analysis of the hemoglobin D component from chicken.,Knapp JE, Oliveira MA, Xie Q, Ernst SR, Riggs AF, Hackert ML J Biol Chem. 1999 Mar 5;274(10):6411-20. PMID:10037733[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Knapp JE, Oliveira MA, Xie Q, Ernst SR, Riggs AF, Hackert ML. The structural and functional analysis of the hemoglobin D component from chicken. J Biol Chem. 1999 Mar 5;274(10):6411-20. PMID:10037733

1hbr, resolution 2.30Å

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