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PDBsum entry 1lfn
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Acta Crystallogr B
47:998
(1991)
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PubMed id:
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Molecular replacement solution of the structure of apolactoferrin, a protein displaying large-scale conformational change.
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G.E.Norris,
B.F.Anderson,
E.N.Baker.
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ABSTRACT
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The crystal structure of an orthorhombic form of human apolactoferrin (ApoLf)
has been determined from 2.8 A diffractometer data by molecular replacement
methods. A variety of search models derived from the diferric lactoferrin
structure (Fe2Lf) were used to obtain a consistent solution to the rotation
function. An R-factor search gave the correct translational solution and the
model was refined by rigid-body least-squares refinement (program CORELS). Only
three of the four domains were located correctly by this procedure, however; the
fourth was finally placed correctly by rotating it manually onto three strands
of electron density which were recognized as part of its central beta-sheet. The
final model, refined by restrained least-squares methods to an R factor of 0.214
for data in the resolution range 10.0 to 2.8 A, shows a large domain movement in
the N-terminal half of the molecule (a 54 degree rotation of domain N2) and
smaller domain movements elsewhere, when compared with Fe2Lf. A feature of the
crystal structure is that although the ApoLf and Fe2Lf unit cells appear very
similar, their crystal packing and molecular structures are quite different.
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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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S.C.Flores,
K.S.Keating,
J.Painter,
F.Morcos,
K.Nguyen,
E.A.Merritt,
L.A.Kuhn,
and
M.B.Gerstein
(2008).
HingeMaster: normal mode hinge prediction approach and integration of complementary predictors.
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Proteins,
73,
299-319.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
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so more and more references will be included with time.
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