2d5x: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /> <applet load="2d5x" size="450" color="white" frame="true" align="right" spinBox="true" caption="2d5x, resolution 1.45Å" /> '''Crystal structure o...
 
No edit summary
 
(16 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2d5x.gif|left|200px]]<br />
<applet load="2d5x" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2d5x, resolution 1.45&Aring;" />
'''Crystal structure of carbonmonoxy horse hemoglobin complexed with L35'''<br />


==Overview==
==Crystal structure of carbonmonoxy horse hemoglobin complexed with L35==
Although detailed crystal structures of haemoglobin (Hb) provide a clear, understanding of the basic allosteric mechanism of the protein, and how, this in turn controls oxygen affinity, recent experiments with artificial, effector molecules have shown a far greater control of oxygen binding than, with natural heterotropic effectors. Contrary to the established text-book, view, these non-physiological compounds are able to reduce oxygen affinity, very strongly without switching the protein to the T (tense) state. In an, earlier paper we showed that bezafibrate (BZF) binds to a surface pocket, on the alpha subunits of R state Hb, strongly reducing the oxygen affinity, of this protein conformation. Here we report the crystallisation of Hb, with L35, a related compound, and show that this binds to the central, cavity of both R and T state Hb. The mechanism by which L35 reduces oxygen, affinity is discussed, in relation to spectroscopic studies of effector, binding.
<StructureSection load='2d5x' size='340' side='right'caption='[[2d5x]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2d5x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D5X 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]] 1.45&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=L35:2-[4-({[(3,5-DICHLOROPHENYL)AMINO]CARBONYL}AMINO)PHENOXY]-2-METHYLPROPANOIC+ACID'>L35</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=2d5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d5x OCA], [https://pdbe.org/2d5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d5x RCSB], [https://www.ebi.ac.uk/pdbsum/2d5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d5x ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HBA_HORSE HBA_HORSE] 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/d5/2d5x_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=2d5x ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2D5X is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with HEM, CMO and L35 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2D5X OCA].
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
R-state haemoglobin with low oxygen affinity: crystal structures of deoxy human and carbonmonoxy horse haemoglobin bound to the effector molecule L35., Yokoyama T, Neya S, Tsuneshige A, Yonetani T, Park SY, Tame JR, J Mol Biol. 2006 Feb 24;356(3):790-801. Epub 2005 Dec 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16403522 16403522]
[[Category: Equus caballus]]
[[Category: Equus caballus]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Neya, S.]]
[[Category: Neya S]]
[[Category: Park, S.Y.]]
[[Category: Park SY]]
[[Category: Tame, J.R.]]
[[Category: Tame JR]]
[[Category: Tsuneshige, A.]]
[[Category: Tsuneshige A]]
[[Category: Yokoyama, T.]]
[[Category: Yokoyama T]]
[[Category: Yonetani, T.]]
[[Category: Yonetani T]]
[[Category: CMO]]
[[Category: HEM]]
[[Category: L35]]
[[Category: allosteric effector]]
[[Category: crystal structure]]
[[Category: hemoglobin]]
[[Category: l35]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov  8 13:29:13 2007''

Latest revision as of 16:46, 13 March 2024

Crystal structure of carbonmonoxy horse hemoglobin complexed with L35Crystal structure of carbonmonoxy horse hemoglobin complexed with L35

Structural highlights

2d5x is a 2 chain structure with sequence from Equus caballus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.45Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HBA_HORSE 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.

See Also

2d5x, resolution 1.45Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=2d5x&oldid=4088655"