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PDBsum entry 1ymh
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Immune system
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PDB id
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1ymh
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Contents |
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220 a.a.
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218 a.a.
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65 a.a.
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* Residue conservation analysis
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PDB id:
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Immune system
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Title:
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Anti-hcv fab 19d9d6 complexed with protein l (ppl) mutant a66w
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Structure:
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Fab 16d9d6, light chain. Chain: a, c. Fab 16d9d6, heavy chain. Chain: b, d. Protein l. Chain: e, f. Synonym: ppl. Engineered: yes. Mutation: yes
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Source:
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Mus musculus. House mouse. Organism_taxid: 10090. Cell_line: hybridoma. Finegoldia magna. Organism_taxid: 334413. Strain: atcc 29328. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Biol. unit:
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Trimer (from
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Resolution:
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2.60Å
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R-factor:
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0.228
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R-free:
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0.302
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Authors:
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V.Granata,N.G.Housden,S.Harrison,C.Jolivet-Reynaud,M.G.Gore,E.A.Stura
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Key ref:
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V.Granata
et al.
(2005).
Comparison of the crystallization and crystal packing of two Fab single-site mutant protein L complexes.
Acta Crystallogr D Biol Crystallogr,
61,
750-754.
PubMed id:
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Date:
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21-Jan-05
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Release date:
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31-May-05
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PROCHECK
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Headers
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References
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No UniProt id for this chain
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Acta Crystallogr D Biol Crystallogr
61:750-754
(2005)
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PubMed id:
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Comparison of the crystallization and crystal packing of two Fab single-site mutant protein L complexes.
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V.Granata,
N.G.Housden,
S.Harrison,
C.Jolivet-Reynaud,
M.G.Gore,
E.A.Stura.
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ABSTRACT
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Protein L from Peptostreptococcus magnus (PpL) is a multidomain protein composed
of four or five immunoglobulin-binding domains that target the kappa light chain
of a large repertoire of human and murine antibodies. Thus, a single domain of
this protein can be used to aid the crystallization of Fab, free or complexed to
their antigen when it is not possible to obtain crystals without it. Each
wild-type PpL domain has two light-chain binding sites that target the same
region of the light chain and can thus bring together two Fab-antigen complexes
within the crystal lattice. In this context the small PpL domain is sandwiched
between two Fab and cannot participate in crystal contacts, thus mutants are
unlikely to increase the chances of crystallizing a particular complex. However,
it is possible to design mutants that can bind at only one site by making use of
the crystal structures obtained so far. Such mutants will have a free surface
that can participate in crystal contacts and that can be modified to improve its
crystal contact-forming properties. Here, a comparison of two single-site
mutants that differ at three different positions is reported. In both mutants
two different tryptophan residues participate in crystal-packing interactions,
suggesting that this residue may be particularly interesting for enhancing
crystal-contact formation.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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H.P.Su,
J.W.Golden,
A.G.Gittis,
J.W.Hooper,
and
D.N.Garboczi
(2007).
Structural basis for the binding of the neutralizing antibody, 7D11, to the poxvirus L1 protein.
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Virology,
368,
331-341.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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}
}
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