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PDBsum entry 1vqh
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DNA binding protein
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PDB id
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1vqh
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Contents |
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* Residue conservation analysis
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Proc Natl Acad Sci U S A
93:10753-10757
(1996)
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PubMed id:
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Potential use of additivity of mutational effects in simplifying protein engineering.
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M.M.Skinner,
T.C.Terwilliger.
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ABSTRACT
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The problem of rationally engineering protein molecules can be simplified where
effects of mutations on protein function are additive. Crystal structures of
single and double mutants in the hydrophobic core of gene V protein indicate
that structural and functional effects of core mutations are additive when the
regions structurally influenced by the mutations do not substantially overlap.
These regions of influence can provide a simple basis for identifying sets of
mutations that will show additive effects.
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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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L.T.Huang,
and
M.M.Gromiha
(2009).
Reliable prediction of protein thermostability change upon double mutation from amino acid sequence.
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Bioinformatics,
25,
2181-2187.
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A.Y.Istomin,
M.M.Gromiha,
O.K.Vorov,
D.J.Jacobs,
and
D.R.Livesay
(2008).
New insight into long-range nonadditivity within protein double-mutant cycles.
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Proteins,
70,
915-924.
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K.S.Goo,
C.S.Chua,
and
T.S.Sim
(2008).
Relevant double mutations in bioengineered Streptomyces clavuligerus deacetoxycephalosporin C synthase result in higher binding specificities which improve penicillin bioconversion.
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Appl Environ Microbiol,
74,
1167-1175.
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M.S.Kim,
J.D.Weaver,
and
X.G.Lei
(2008).
Assembly of mutations for improving thermostability of Escherichia coli AppA2 phytase.
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Appl Microbiol Biotechnol,
79,
751-758.
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A.Kun,
M.Santos,
and
E.Szathmáry
(2005).
Real ribozymes suggest a relaxed error threshold.
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Nat Genet,
37,
1008-1011.
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R.K.Jain,
and
R.Ranganathan
(2004).
Local complexity of amino acid interactions in a protein core.
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Proc Natl Acad Sci U S A,
101,
111-116.
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PDB codes:
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B.J.McFarland,
and
C.Beeson
(2002).
Binding interactions between peptides and proteins of the class II major histocompatibility complex.
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Med Res Rev,
22,
168-203.
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W.P.Russ,
and
R.Ranganathan
(2002).
Knowledge-based potential functions in protein design.
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Curr Opin Struct Biol,
12,
447-452.
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C.Grosman,
and
A.Auerbach
(2000).
Kinetic, mechanistic, and structural aspects of unliganded gating of acetylcholine receptor channels: a single-channel study of second transmembrane segment 12' mutants.
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J Gen Physiol,
115,
621-635.
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C.Grosman,
and
A.Auerbach
(2000).
Asymmetric and independent contribution of the second transmembrane segment 12' residues to diliganded gating of acetylcholine receptor channels: a single-channel study with choline as the agonist.
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J Gen Physiol,
115,
637-651.
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T.Aita,
H.Uchiyama,
T.Inaoka,
M.Nakajima,
T.Kokubo,
and
Y.Husimi
(2000).
Analysis of a local fitness landscape with a model of the rough Mt. Fuji-type landscape: application to prolyl endopeptidase and thermolysin.
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Biopolymers,
54,
64-79.
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B.Spiller,
A.Gershenson,
F.H.Arnold,
and
R.C.Stevens
(1999).
A structural view of evolutionary divergence.
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Proc Natl Acad Sci U S A,
96,
12305-12310.
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PDB codes:
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V.Sieber,
A.Plückthun,
and
F.X.Schmid
(1998).
Selecting proteins with improved stability by a phage-based method.
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Nat Biotechnol,
16,
955-960.
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P.Kast,
and
D.Hilvert
(1997).
3D structural information as a guide to protein engineering using genetic selection.
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Curr Opin Struct Biol,
7,
470-479.
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S.Su,
Y.G.Gao,
H.Zhang,
T.C.Terwilliger,
and
A.H.Wang
(1997).
Analyses of the stability and function of three surface mutants (R82C, K69H, and L32R) of the gene V protein from Ff phage by X-ray crystallography.
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Protein Sci,
6,
771-780.
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PDB codes:
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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
codes are
shown on the right.
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Links
