The quaternary structure of carbonmonoxy hemoglobin ypsilanti.
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.
Janin
J
J
Laboratoire de Biologie Structurale UMR 9920-CNRS, Université Paris-Sud, Orsay, France.
Wodak
S J
SJ
D000494:Allosteric Regulation; D002263:Carboxyhemoglobin / Q000737:chemistry*; D003198:Computer Simulation; D006455:Hemoglobins, Abnormal / Q000737:chemistry*; D008956:Models, Chemical; D011487:Protein Conformation
D006455:Hemoglobins, Abnormal; D002263:Carboxyhemoglobin; C070942:hemoglobin Ypsilanti