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The crystal structures of trout Hb I in the deoxy and carbonmonoxy forms.

Abstract：

: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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Tame JR,Wilson JC,Weber RE

doi

10.1006/jmbi.1996.0355

subject

Has Abstract

pub_date

1996-06-21 00:00:00

pages

749-60

issue

4

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(96)90355-1

journal_volume

259

pub_type

杂志文章

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