Abstract：
:The three-dimensional structure of the 66-amino acid cro repressor protein of bacteriophage lambda suggests how it binds to its operator DNA. We propose that a dimer of cro protein is bound to the B-form of DNA with the 2-fold axis of the dimer coincident with the 2-fold axis of DNA. A pair of 2-fold-related alpha-helices of the repressor, lying within successive major grooves of the DNA, seem to be a major determinant in recognition and binding. In addition, the C-terminal residues of the protein, some of which are disordered in the absence of DNA, appear to contribute to the binding.
journal_name
Naturejournal_title
Natureauthors
Anderson WF,Ohlendorf DH,Takeda Y,Matthews BWdoi
10.1038/290754a0subject
Has Abstractpub_date
1981-04-30 00:00:00pages
754-8issue
5809eissn
0028-0836issn
1476-4687journal_volume
290pub_type
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