Crystal Structure of a Five Site Mutated Cyanovirin-N with a Mannose Dimer Bound at 1.8 A Resolution

Raimund Fromme (Contributor)
Zivile Katiliene (Contributor)
Barbara Giomarelli (Contributor)
Federica Bogani (Contributor)
James B. McMahon (Contributor)
Toshiyuki Mori (Contributor)
Petra Fromme (Contributor)
Giovanna Ghirlanda (Contributor)

Dataset

Date made available	Jul 31 2007
Publisher	Protein Data Bank (PDB)

DOI
10.2210/pdb2PYS/pdb

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https://www.wwpdb.org/pdb?id=pdb_00002pys

1 Article

A monovalent mutant of cyanovirin-N provides insight into the role of multiple interactions with gp120 for antiviral activity
Fromme, R., Katiliene, Z., Giomarelli, B., Bogani, F., Mc Mahon, J., Mori, T., Fromme, P. & Ghirlanda, G., Aug 14 2007, In: Biochemistry. 46, 32, p. 9199-9207 9 p.
Research output: Contribution to journal › Article › peer-review
38 Scopus citations

Cite this

Fromme, R. (Contributor), Katiliene, Z. (Contributor), Giomarelli, B. (Contributor), Bogani, F. (Contributor), Mc Mahon, J. (Contributor), Mori, T. (Contributor), Fromme, P. (Contributor), Ghirlanda, G. (Contributor) (Jul 31 2007). Crystal Structure of a Five Site Mutated Cyanovirin-N with a Mannose Dimer Bound at 1.8 A Resolution. Protein Data Bank (PDB). 10.2210/pdb2PYS/pdb

Crystal Structure of a Five Site Mutated Cyanovirin-N with a Mannose Dimer Bound at 1.8 A Resolution

DOI

Access Dataset

Research output

A monovalent mutant of cyanovirin-N provides insight into the role of multiple interactions with gp120 for antiviral activity

Cite this