1out
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(New page: 200px<br /> <applet load="1out" size="450" color="white" frame="true" align="right" spinBox="true" caption="1out, resolution 2.3Å" /> '''TROUT HEMOGLOBIN I''...)
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Revision as of 11:09, 8 November 2007
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TROUT HEMOGLOBIN I
Overview
We have determined the X-ray crystallographic structure of trout Hb I in, both the deoxy and carbonmonoxy forms to resolution limits of 2.3, angstroms and 2.5 angstroms, respectively. The overall fold of the, molecule is highly similar to that of human HbA despite the low level of, sequence identity between these proteins. Trout Hb I is unusual in, displaying almost no pH dependence of oxygen binding affinity, and (at, most) very weak interactions with heterotropic effector ligands such as, organic phosphates. Comparison of the two quaternary states of the protein, indicates how such effects are minimised and how the low-affinity T state, of the protein is stabilised in the absence of heterotropic interactions.
About this Structure
1OUT is a Protein complex structure of sequences from Oncorhynchus mykiss with ACE and HEM as ligands. Full crystallographic information is available from OCA.
Reference
The crystal structures of trout Hb I in the deoxy and carbonmonoxy forms., Tame JR, Wilson JC, Weber RE, J Mol Biol. 1996 Jun 21;259(4):749-60. PMID:8683580
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