|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Cell adhesion
|
|
|
Title:
|
|
Crystal structure of a sparc-collagen complex
|
|
Structure:
|
|
Sparc. Chain: a. Fragment: fs and ec domains, residues 70-212,221-303. Synonym: secreted protein acidic and rich in cysteine, osteonectin, on, basement-membrane protein 40, bm-40. Engineered: yes. Collagen alpha-1(iii) chain. Chain: b, c, d. Fragment: residues 564-584.
|
|
Source:
|
|
Homo sapiens. Human. Organism_taxid: 9606. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: 293-ebna. Synthetic: yes. Organism_taxid: 9606
|
|
Resolution:
|
|
|
3.20Å
|
R-factor:
|
0.261
|
R-free:
|
0.320
|
|
|
Authors:
|
|
E.Hohenester,T.Sasaki,C.Giudici,R.W.Farndale,H.P.Bachinger
|
Key ref:
|
|
E.Hohenester
et al.
(2008).
Structural basis of sequence-specific collagen recognition by SPARC.
Proc Natl Acad Sci U S A,
105,
18273-18277.
PubMed id:
DOI:
|
|
|
Date:
|
|
|
01-Oct-08
|
Release date:
|
25-Nov-08
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
Proc Natl Acad Sci U S A
105:18273-18277
(2008)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Structural basis of sequence-specific collagen recognition by SPARC.
|
|
E.Hohenester,
T.Sasaki,
C.Giudici,
R.W.Farndale,
H.P.Bächinger.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
Protein interactions with the collagen triple helix play a critical role in
collagen fibril formation, cell adhesion, and signaling. However, structural
insight into sequence-specific collagen recognition is limited to an
integrin-peptide complex. A GVMGFO motif in fibrillar collagens (O denotes
4-hydroxyproline) binds 3 unrelated proteins: von Willebrand factor (VWF),
discoidin domain receptor 2 (DDR2), and the extracellular matrix protein
SPARC/osteonectin/BM-40. We report the crystal structure at 3.2 A resolution of
human SPARC bound to a triple-helical 33-residue peptide harboring the
promiscuous GVMGFO motif. SPARC recognizes the GVMGFO motifs of the middle and
trailing collagen chains, burying a total of 720 A(2) of solvent-accessible
collagen surface. SPARC binding does not distort the canonical triple helix of
the collagen peptide. In contrast, a critical loop in SPARC is substantially
remodelled upon collagen binding, creating a deep pocket that accommodates the
phenylalanine residue of the trailing collagen chain ("Phe pocket"). This highly
restrictive specificity pocket is shared with the collagen-binding integrin
I-domains but differs strikingly from the shallow collagen-binding grooves of
the platelet receptor glycoprotein VI and microbial adhesins. We speculate that
binding of the GVMGFO motif to VWF and DDR2 also results in structural changes
and the formation of a Phe pocket.
|
|
|
|
|
|
| |
Selected figure(s)
|
|
|
|
| |
|
|
|
|
|
|
Figure 1.
Crystal structure of SPARC FS-EC ΔαC bound to a 33-residue
collagen peptide (stereoview). The FS and EC domains of SPARC
are in green and cyan, respectively. Disulphide bridges are in
pale pink, the glycan attached to N99 is in gray, and a calcium
ion is shown as a purple sphere. The collagen peptide is shown
as a Cα ribbon (leading chain, yellow; middle chain, orange;
trailing chain, red). The chain termini, selected helices and
the location of the αC deletion are labeled.
|
|
Figure 4.
Putative SPARC-binding sites in collagen IV. Shown are
partial sequences of human collagen III (SwissProt entry P02461)
and collagen IV (α1 chain, P02462; α2 chain, P08572). The
SPARC-binding site in collagen III is highlighted; residues that
are predicted to be strictly required for SPARC binding (see
Prediction of SPARC-Binding Sites in Collagens I–IV) are in
red, residues that should be apolar are in orange. The same
coloring scheme is used to indicate the 4 putative SPARC-binding
sites in collagen IV.
|
|
|
|
| |
Figures were
selected
by an automated process.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
H.Xu,
N.Raynal,
S.Stathopoulos,
J.Myllyharju,
R.W.Farndale,
and
B.Leitinger
(2011).
Collagen binding specificity of the discoidin domain receptors: binding sites on collagens II and III and molecular determinants for collagen IV recognition by DDR1.
|
| |
Matrix Biol,
30,
16-26.
|
|
|
|
|
|
|
J.D.Parkin,
J.D.San Antonio,
V.Pedchenko,
B.Hudson,
S.T.Jensen,
and
J.Savige
(2011).
Mapping structural landmarks, ligand binding sites, and missense mutations to the collagen IV heterotrimers predicts major functional domains, novel interactions, and variation in phenotypes in inherited diseases affecting basement membranes.
|
| |
Hum Mutat,
32,
127-143.
|
|
|
|
|
|
|
L.Vitagliano,
R.Berisio,
and
A.De Simone
(2011).
Role of hydration in collagen recognition by bacterial adhesins.
|
| |
Biophys J,
100,
2253-2261.
|
|
|
|
|
|
|
M.H.Huynh,
S.J.Zhu,
A.Kollara,
T.Brown,
R.Winklbauer,
and
M.Ringuette
(2011).
Knockdown of SPARC leads to decreased cell-cell adhesion and lens cataracts during post-gastrula development in Xenopus laevis.
|
| |
Dev Genes Evol,
220,
315-327.
|
|
|
|
|
|
|
S.Niland,
C.Westerhausen,
S.W.Schneider,
B.Eckes,
M.F.Schneider,
and
J.A.Eble
(2011).
Biofunctionalization of a generic collagenous triple helix with the α2β1 integrin binding site allows molecular force measurements.
|
| |
Int J Biochem Cell Biol,
43,
721-731.
|
|
|
|
|
|
|
A.Chlenski,
and
S.L.Cohn
(2010).
Modulation of matrix remodeling by SPARC in neoplastic progression.
|
| |
Semin Cell Dev Biol,
21,
55-65.
|
|
|
|
|
|
|
G.B.Fields
(2010).
Synthesis and biological applications of collagen-model triple-helical peptides.
|
| |
Org Biomol Chem,
8,
1237-1258.
|
|
|
|
|
|
|
J.A.Fallas,
L.E.O'Leary,
and
J.D.Hartgerink
(2010).
Synthetic collagen mimics: self-assembly of homotrimers, heterotrimers and higher order structures.
|
| |
Chem Soc Rev,
39,
3510-3527.
|
|
|
|
|
|
|
J.Emsley
(2010).
Convergent recognition of a triple helical hydrophobic motif in collagen.
|
| |
Structure,
18,
1-2.
|
|
|
|
|
|
|
T.H.Brondijk,
T.de Ruiter,
J.Ballering,
H.Wienk,
R.J.Lebbink,
H.van Ingen,
R.Boelens,
R.W.Farndale,
L.Meyaard,
and
E.G.Huizinga
(2010).
Crystal structure and collagen-binding site of immune inhibitory receptor LAIR-1: unexpected implications for collagen binding by platelet receptor GPVI.
|
| |
Blood,
115,
1364-1373.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
T.van Wieringen,
S.Kalamajski,
A.Lidén,
D.Bihan,
B.Guss,
D.Heinegård,
R.W.Farndale,
and
K.Rubin
(2010).
The streptococcal collagen-binding protein CNE specifically interferes with alphaVbeta3-mediated cellular interactions with triple helical collagen.
|
| |
J Biol Chem,
285,
35803-35813.
|
|
|
|
|
|
|
U.Venkatraman Girija,
C.Furze,
J.Toth,
W.J.Schwaeble,
D.A.Mitchell,
A.H.Keeble,
and
R.Wallis
(2010).
Engineering novel complement activity into a pulmonary surfactant protein.
|
| |
J Biol Chem,
285,
10546-10552.
|
|
|
|
|
|
|
A.B.Herr,
and
R.W.Farndale
(2009).
Structural insights into the interactions between platelet receptors and fibrillar collagen.
|
| |
J Biol Chem,
284,
19781-19785.
|
|
|
|
|
|
|
A.D.Bradshaw
(2009).
The role of SPARC in extracellular matrix assembly.
|
| |
J Cell Commun Signal,
3,
239-246.
|
|
|
|
|
|
|
A.Koehler,
S.Desser,
B.Chang,
J.MacDonald,
U.Tepass,
and
M.Ringuette
(2009).
Molecular evolution of SPARC: absence of the acidic module and expression in the endoderm of the starlet sea anemone, Nematostella vectensis.
|
| |
Dev Genes Evol,
219,
509-521.
|
|
|
|
|
|
|
F.Carafoli,
D.Bihan,
S.Stathopoulos,
A.D.Konitsiotis,
M.Kvansakul,
R.W.Farndale,
B.Leitinger,
and
E.Hohenester
(2009).
Crystallographic insight into collagen recognition by discoidin domain receptor 2.
|
| |
Structure,
17,
1573-1581.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
J.Nie,
and
E.H.Sage
(2009).
SPARC functions as an inhibitor of adipogenesis.
|
| |
J Cell Commun Signal,
3,
247-254.
|
|
|
|
|
|
|
M.M.Phelan,
C.T.Thai,
D.C.Soares,
R.T.Ogata,
P.N.Barlow,
and
J.Bramham
(2009).
Solution structure of factor I-like modules from complement C7 reveals a pair of follistatin domains in compact pseudosymmetric arrangement.
|
| |
J Biol Chem,
284,
19637-19649.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
S.Liao,
M.Ngiam,
C.K.Chan,
and
S.Ramakrishna
(2009).
Fabrication of nano-hydroxyapatite/collagen/osteonectin composites for bone graft applications.
|
| |
Biomed Mater,
4,
25019.
|
|
|
|
|
|
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.
|
 |
Links
