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PDBsum entry 2igf
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Immunoglobulin
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PDB id
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2igf
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structures of an antibody to a peptide and its complex with peptide antigen at 2.8 a.
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Authors
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R.L.Stanfield,
T.M.Fieser,
R.A.Lerner,
I.A.Wilson.
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Ref.
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Science, 1990,
248,
712-719.
[DOI no: ]
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PubMed id
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Abstract
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The three-dimensional structures of an antibody to a peptide and its complex
with the peptide antigen have been determined at 2.8 A resolution. The antigen
is a synthetic 19-amino acid peptide homolog of the C helix of myohemerythrin
(Mhr). The unliganded Fab' crystals are orthorhombic with two molecules per
asymmetric unit, whereas the complex crystals are hexagonal with one molecule
per asymmetric unit. The Fab' and the Fab'-peptide complex structures have been
solved independently by molecular replacement methods and have crystallographic
R factors of 0.197 and 0.215, respectively, with no water molecules included.
The amino-terminal portion of the peptide sequence
(NH2-Glu-Val-Val-Pro-His-Lys-Lys) is clearly interpretable in the electron
density map of the Fab'-peptide complex and adopts a well-defined type II
beta-turn in the concave antigen binding pocket. This same peptide amino acid
sequence in native Mhr is alpha-helical. The peptide conformation when bound to
the Fab' is inconsistent with binding of the Fab' to native Mhr, and suggests
that binding of the Fab' to conformationally altered forms of the native Mhr or
to apo-Mhr. Immunological mapping previously identified this sequence as the
peptide epitope, and its fine specificity correlates well with the structural
analysis. The binding pocket includes a large percentage of hydrophobic
residues. The buried surfaces of the peptide and the antibody are complementary
in shape and cover 460 A2 and 540 A2, respectively. These two structures now
enable a comparison of a specific monoclonal Fab' both in its free and antigen
complexed state. While no major changes in the antibody were observed when
peptide was bound, there were some small but significant side chain and main
chain rearrangements.
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Secondary reference #1
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Title
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Preliminary crystallographic data and primary sequence for anti-Peptide FAB' B13i2 and its complex with the c-Helix peptide from myohemerythrin.
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Authors
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E.A.Stura,
R.L.Stanfield,
T.M.Fieser,
R.S.Balderas,
L.R.Smith,
R.A.Lerner,
I.A.Wilson.
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Ref.
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J Biol Chem, 1989,
264,
15721-15725.
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PubMed id
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