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PDBsum entry 1kth
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Structural protein
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PDB id
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1kth
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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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Anisotropic behaviour of the c-Terminal kunitz-Type domain of the alpha3 chain of human type vi collagen at atomic resolution (0.9 a).
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Authors
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B.Arnoux,
A.Ducruix,
T.Prangé.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2002,
58,
1252-1254.
[DOI no: ]
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PubMed id
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Abstract
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The C-terminal Kunitz-type domain from the alpha3 chain of human type VI
collagen (C5), a single amino-acid residue chain with three disulfide bridges,
was refined at 0.9 A resolution in a monoclinic form, space group P2(1) with one
molecule per asymmetric unit, using data collected at cryogenic temperature (110
K). The average protein factor decreases from 21 A(2) at room temperature (RT)
to 12 A(2) at cryotemperature (100 K, CT). The spatially close N- and C-termini
remain highly disordered. The different structural motifs of C5 were analyzed in
terms of rigid-body displacement (TLS analyses) and show dominant libration
motion for the secondary structure.
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Figure 1.
Figure 1 (a) Comparison between room-temperature (RT, red) and
cryotemperature (CT, blue) average factors in residues. The
residual factors after correction from a rigid-body motion
are also displayed as a green curve. (b) MOLSCRIPT/RASMOL
representation of the anisotropic structure (Kraulis,
1991[Kraulis, P. E. (1991). J. Appl. Cryst. 24, 946-950.];
Merritt & Bacon, 1997[Merritt, E. A. & Bacon, D. J. (1997).
Methods Enzymol. 277, 505-524.]). The ellipsoids are
colour-coded from blue to red over the range 4-40 Å2.
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The above figure is
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2002,
58,
1252-1254)
copyright 2002.
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Secondary reference #1
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Title
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The 1.6 a structure of kunitz-Type domain from the alpha 3 chain of human type VI collagen.
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Authors
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B.Arnoux,
K.Mérigeau,
P.Saludjian,
F.Norris,
K.Norris,
S.Bjørn,
O.Olsen,
L.Petersen,
A.Ducruix.
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Ref.
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J Mol Biol, 1995,
246,
609-617.
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PubMed id
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Secondary reference #2
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Title
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1.2 a refinement of the kunitz-Type domain from the alpha3 chain of human type VI collagen.
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Authors
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K.Merigeau,
B.Arnoux,
D.Perahia,
K.Norris,
F.Norris,
A.Ducruix.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1998,
54,
306-312.
[DOI no: ]
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PubMed id
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Figure 2.
Figure 2 Modeling of Phe17 environment of C5 (red) superimposed
with the BPTI molecule of the trypsin (black)/BPTI (blue)
complex (2PTC) showing prohibited van der Waals contacts.
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Figure 4.
Figure 4 Alternate conformations of (a) Thr2, (b) Asp3, (c)
Thr13, (d) Asp16 and (e) Ile18 deduced from the 2F[o] - F[c]
electron-density map (1  ).
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The above figures are
reproduced from the cited reference
with permission from the IUCr
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