The quaternary structure of carbonmonoxy hemoglobin ypsilanti | Zendy

Janin Joël | Zendy; Wodak Shoshana J. | Zendy

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The quaternary structure of carbonmonoxy hemoglobin ypsilanti

Author(s) -

Janin Joël,

Wodak Shoshana J.

Publication year - 1993

Publication title -

proteins: structure, function, and bioinformatics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.699

H-Index - 191

eISSN - 1097-0134

pISSN - 0887-3585

DOI - 10.1002/prot.340150102

Subject(s) - protein quaternary structure , quaternary , dimer , allosteric regulation , chemistry , crystallography , hemoglobin , rotation (mathematics) , stereochemistry , mathematics , geometry , geology , protein subunit , biochemistry , paleontology , organic chemistry , gene , enzyme

We present a geometric analysis of the allosteric interface in the new Y state quaternary structure observed in liganded mutant hemoglobin Ypsilanti (β99 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 αβ dimers about an axis which is approximately parallel to the dimer axis of pseudosym‐metry, 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. © 1993 Wiley‐Liss, Inc.

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