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PDBsum entry 2erf
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Sugar binding protein
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PDB id
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2erf
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References listed in PDB file
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Key reference
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Title
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The structures of the thrombospondin-1 n-Terminal domain and its complex with a synthetic pentameric heparin.
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Authors
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K.Tan,
M.Duquette,
J.H.Liu,
R.Zhang,
A.Joachimiak,
J.H.Wang,
J.Lawler.
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Ref.
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Structure, 2006,
14,
33-42.
[DOI no: ]
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PubMed id
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Abstract
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The N-terminal domain of thrombospondin-1 (TSPN-1) mediates the protein's
interaction with (1) glycosaminoglycans, calreticulin, and integrins during
cellular adhesion, (2) low-density lipoprotein receptor-related protein during
uptake and clearance, and (3) fibrinogen during platelet aggregation. The
crystal structure of TSPN-1 to 1.8 A resolution is a beta sandwich with 13
antiparallel beta strands and 1 irregular strand-like segment. Unique structural
features of the N- and C-terminal regions, and the disulfide bond location,
distinguish TSPN-1 from the laminin G domain and other concanavalin A-like
lectins/glucanases superfamily members. The crystal structure of the complex of
TSPN-1 with heparin indicates that residues R29, R42, and R77 in an extensive
positively charged patch at the bottom of the domain specifically associate with
the sulfate groups of heparin. The TSPN-1 structure and identified adjacent
linker region provide a structural framework for the analysis of the TSPN domain
of various molecules, including TSPs, NELLs, many collagens, TSPEAR, and kielin.
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Figure 4.
Figure 4. The Topology of TSPN-1
The topology of (A)
TSPN-1 is compared with that of (B) CTSP-1 (the C-terminal
domain of TSP-1) (Kvansakul et al., 2004) and (C) a typical LG
(Laminin A G-domain [LG]/Neurexin/Sex hormone binding globulin
[SHBG]) repeat (Rudenko et al., 2001). For the LG structure,
only the common positions of the b strands are shown. The
disulfide bonds are highlighted in yellow. Only b strands (cyan)
are labeled for comparison. The a helices of TSPN-1 and CTSP-1
are shown in green. The two structures can't be simply
superimposed. The best alignment can only be made with the
middle strands of the back sheet, b14, b5, b10, and b11 of
TSPN-1 and b15, b5, b11, and b12 of CTSP-1. Even in this
alignment, the b strands from the two front sheets shift over
about one strand and also rotate slightly. The edge strands,
especially the N-terminal edge strands, are totally out of
alignment. The front concaved sheet of CTSP-1 is distinctly
curved, while that of TSPN-1 is relatively flat.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2006,
14,
33-42)
copyright 2006.
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