The quaternary structure of carbonmonoxy hemoglobin ypsilanti.

TitleThe quaternary structure of carbonmonoxy hemoglobin ypsilanti.
Publication TypeJournal Article
Year of Publication1993
AuthorsJanin, J., and S. J. Wodak
Date Published1993 Jan
KeywordsAllosteric Regulation, Carboxyhemoglobin, Computer Simulation, Hemoglobins, Abnormal, Models, Chemical, Protein Conformation

We present a geometric analysis of the allosteric interface in the new Y state quaternary structure observed in liganded mutant hemoglobin Ypsilanti (beta 99 Asp-->Tyr) by Smith, F.R., Lattman, E.E., Carter, C.W., Jr. (Proteins 10:81-91, 1991). The classical T to R quaternary structure change being a rotation of alpha beta dimers about an axis which is approximately parallel to the dimer axis of pseudosymmetry, the new quaternary structure is obtained by applying to R an additional rotation about an axis orthogonal to the first. This suggests that Y is a modified R state rather than an intermediate on the T to R pathway. Computer docking experiments designed to simulate the quaternary structure change support this suggestion.

Alternate JournalProteins
PubMed ID8451234