1hgb

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{{STRUCTURE_1hgb| PDB=1hgb | SCENE= }}
{{STRUCTURE_1hgb| PDB=1hgb | SCENE= }}
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'''HIGH RESOLUTION CRYSTAL STRUCTURES AND COMPARISONS OF T STATE DEOXYHAEMOGLOBIN AND TWO LIGANDED T-STATE HAEMOGLOBINS: T(ALPHA-OXY)HAEMOGLOBIN AND T(MET)HAEMOGLOBIN'''
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===HIGH RESOLUTION CRYSTAL STRUCTURES AND COMPARISONS OF T STATE DEOXYHAEMOGLOBIN AND TWO LIGANDED T-STATE HAEMOGLOBINS: T(ALPHA-OXY)HAEMOGLOBIN AND T(MET)HAEMOGLOBIN===
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==Overview==
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The origin of co-operativity in haemoglobin (Hb) resides in the reduced affinity of the T-state. T-state Hb crystals grown from polyethyleneglycol can be liganded without the molecule switching to the R high affinity state. X-ray analysis of T-state alpha-oxy Hb and T-state met Hb has identified the structural basis for reduced affinity. The nature of the chemical tension at the haem environment is different in the alpha and beta haems. There are small but definite structural changes associated with ligation in the T-state: these prove to be mostly in the same direction as the larger changes that occur in the T--&gt;R transition.
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(as it appears on PubMed at http://www.pubmed.gov), where 1453464 is the PubMed ID number.
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{{ABSTRACT_PUBMED_1453464}}
==About this Structure==
==About this Structure==
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[[Category: Liddington, R.]]
[[Category: Liddington, R.]]
[[Category: Oxygen transport]]
[[Category: Oxygen transport]]
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Revision as of 05:09, 1 July 2008

Image:1hgb.png

Template:STRUCTURE 1hgb

HIGH RESOLUTION CRYSTAL STRUCTURES AND COMPARISONS OF T STATE DEOXYHAEMOGLOBIN AND TWO LIGANDED T-STATE HAEMOGLOBINS: T(ALPHA-OXY)HAEMOGLOBIN AND T(MET)HAEMOGLOBIN

Template:ABSTRACT PUBMED 1453464

About this Structure

1HGB is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

High resolution crystal structures and comparisons of T-state deoxyhaemoglobin and two liganded T-state haemoglobins: T(alpha-oxy)haemoglobin and T(met)haemoglobin., Liddington R, Derewenda Z, Dodson E, Hubbard R, Dodson G, J Mol Biol. 1992 Nov 20;228(2):551-79. PMID:1453464

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