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PDBsum entry 4z9k
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Hydrolase/immune system
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PDB id
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4z9k
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References listed in PDB file
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Key reference
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Title
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Structural analysis of nested neutralizing and non-Neutralizing b cell epitopes on ricin toxin'S enzymatic subunit.
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Authors
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M.J.Rudolph,
D.J.Vance,
M.S.Cassidy,
Y.Rong,
C.B.Shoemaker,
N.J.Mantis.
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Ref.
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Proteins, 2016,
84,
1162-1172.
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PubMed id
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Abstract
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In this report, we describe the X-ray crystal structures of two single domain
camelid antibodies (VH H), F5 and F8, each in complex with ricin toxin's
enzymatic subunit (RTA). F5 has potent toxin-neutralizing activity, while F8 has
weak neutralizing activity. F5 buried a total of 1760 Å(2) in complex with RTA
and made contact with three prominent secondary structural elements: α-helix B
(Residues 98-106), β-strand h (Residues 113-117), and the C-terminus of
α-helix D (Residues 154-156). F8 buried 1103 Å(2) in complex with RTA that was
centered primarily on β-strand h. As such, the structural epitope of F8 is
essentially nested within that of F5. All three of the F5 complementarity
determining regions CDRs were involved in RTA contact, whereas F8 interactions
were almost entirely mediated by CDR3, which essentially formed a seventh
β-strand within RTA's centrally located β-sheet. A comparison of the two
structures reported here to several previously reported (RTA-VH H) structures
identifies putative contact sites on RTA, particularly α-helix B, associated
with potent toxin-neutralizing activity. This information has implications for
rational design of RTA-based subunit vaccines for biodefense. Proteins 2016;
84:1162-1172. © 2016 Wiley Periodicals, Inc.
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Secondary reference #1
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Title
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Cloning, Purification, Crystallization and 1.57 å resolution X-Ray data analysis of amsi, The tyrosine phosphatase controlling amylovoran biosynthesis in the plant pathogen erwinia amylovora.
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Authors
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S.Benini,
L.Caputi,
M.Cianci.
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Ref.
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Acta Crystallogr F Struct Biol Commun, 2014,
70,
1693-1696.
[DOI no: ]
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PubMed id
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