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Collagen-binding PDB id
1ao3
Jmol
Contents
Protein chains
187 a.a. *
Waters ×169
* Residue conservation analysis
PDB id:
1ao3
Name: Collagen-binding
Title: A3 domain of von willebrand factor
Structure: Von willebrand factor. Chain: a, b. Fragment: a3 domain. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.20Å     R-factor:   0.158     R-free:   0.215
Authors: J.Bienkowski,M.Cruz,R.Handin,R.Liddington
Key ref:
J.Bienkowska et al. (1997). The von willebrand factor A3 domain does not contain a metal ion-dependent adhesion site motif. J Biol Chem, 272, 25162-25167. PubMed id: 9312128 DOI: 10.1074/jbc.272.40.25162
Date:
16-Jul-97     Release date:   22-Jul-98    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P04275  (VWF_HUMAN) -  von Willebrand factor
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		2813 a.a.
187 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1074/jbc.272.40.25162 J Biol Chem 272:25162-25167 (1997)
PubMed id: 9312128  
 
 
The von willebrand factor A3 domain does not contain a metal ion-dependent adhesion site motif.
J.Bienkowska, M.Cruz, A.Atiemo, R.Handin, R.Liddington.
 
  ABSTRACT  
 
von Willebrand factor (vWF) is a multimeric plasma protein that mediates platelet adhesion to exposed subendothelium at sites of vascular injury. The A3 domain of vWF (vWF-A3) forms the principal binding site for collagens type I and III. We report here the crystal structure of the vWF-A3 domain at 2.2-A resolution. As expected, the structure is similar to the integrin I domain but with several novel features. Sequence alignments had suggested that the domain contained an integrin metal ion-dependent adhesion site (MIDAS) motif, but the crystal structure shows that the motif is modified and that no metal ion is bound. We have introduced mutations into the vestigial MIDAS motif and report that, unlike the I domain of integrin alpha2beta1, vWF-A3 continues to bind collagen after disruption of the motif. We conclude that collagen recognition by vWF-A3 occurs by a mechanism different from that of the integrin alpha2beta1.
 
  Selected figure(s)  
 
Figure 3.
Fig. 3. Stereo diagram of the vWF-A3 vestigial MIDAS motif, with schematic main chain and ball-and-stick side chains. The water molecule is labeled W, with hydrogen bonds as dashed red lines. Drawn with MOLSCRIPT (25), RASTER3D (26), and RENDER (27). 		Figure 4.
Fig. 4. The effect of mutations in the vestigial MIDAS motif on collagen binding. Percentage of normal binding to immobilized^ type I collagen detected by enzyme-linked immunosorbent assay.
 
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (1997, 272, 25162-25167) copyright 1997.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21326273 A.P.Hendrickx, J.M.Budzik, S.Y.Oh, and O.Schneewind (2011).
Architects at the bacterial surface - sortases and the assembly of pili with isopeptide bonds.
  Nat Rev Microbiol, 9, 166-176.  
21163365 A.R.Klatt, A.K.Becker, C.D.Neacsu, M.Paulsson, and R.Wagener (2011).
The matrilins: modulators of extracellular matrix assembly.
  Int J Biochem Cell Biol, 43, 320-330.  
21057832 M.Nakajima, Y.Miyamoto, and S.Ikegawa (2011).
Cloning and characterization of the osteoarthritis-associated gene DVWA.
  J Bone Miner Metab, 29, 300-308.  
20152144 J.Emsley (2010).
Convergent recognition of a triple helical hydrophobic motif in collagen.
  Structure, 18, 1-2.  
20152157 T.Izoré, C.Contreras-Martel, L.El Mortaji, C.Manzano, R.Terrasse, T.Vernet, A.M.Di Guilmi, and A.Dessen (2010).
Structural basis of host cell recognition by the pilus adhesin from Streptococcus pneumoniae.
  Structure, 18, 106-115.
PDB code: 2ww8
19318682 S.F.De Meyer, H.Deckmyn, and K.Vanhoorelbeke (2009).
von Willebrand factor to the rescue.
  Blood, 113, 5049-5057.  
19011090 E.Hohenester, T.Sasaki, C.Giudici, R.W.Farndale, and H.P.Bächinger (2008).
Structural basis of sequence-specific collagen recognition by SPARC.
  Proc Natl Acad Sci U S A, 105, 18273-18277.
PDB code: 2v53
18587047 N.S.Seo, C.Q.Zeng, J.M.Hyser, B.Utama, S.E.Crawford, K.J.Kim, M.Höök, and M.K.Estes (2008).
Inaugural article: integrins alpha1beta1 and alpha2beta1 are receptors for the rotavirus enterotoxin.
  Proc Natl Acad Sci U S A, 105, 8811-8818.  
17389010 C.Martin, L.D.Morales, and M.A.Cruz (2007).
Purified A2 domain of von Willebrand factor binds to the active conformation of von Willebrand factor and blocks the interaction with platelet glycoprotein Ibalpha.
  J Thromb Haemost, 5, 1363-1370.  
17600523 L.Shapiro, J.Love, and D.R.Colman (2007).
Adhesion molecules in the nervous system: structural insights into function and diversity.
  Annu Rev Neurosci, 30, 451-474.  
16420575 L.D.Morales, C.Martin, and M.A.Cruz (2006).
The interaction of von Willebrand factor-A1 domain with collagen: mutation G1324S (type 2M von Willebrand disease) impairs the conformational change in A1 domain induced by collagen.
  J Thromb Haemost, 4, 417-425.  
17098186 T.A.Springer (2006).
Complement and the multifaceted functions of VWA and integrin I domains.
  Structure, 14, 1611-1616.  
16102037 J.F.Dong (2005).
Cleavage of ultra-large von Willebrand factor by ADAMTS-13 under flow conditions.
  J Thromb Haemost, 3, 1710-1716.  
15016353 A.A.Bhattacharya, M.L.Lupher, D.E.Staunton, and R.C.Liddington (2004).
Crystal structure of the A domain from complement factor B reveals an integrin-like open conformation.
  Structure, 12, 371-378.
PDB code: 1q0p
12447349 N.Nishida, H.Sumikawa, M.Sakakura, N.Shimba, H.Takahashi, H.Terasawa, E.Suzuki, and I.Shimada (2003).
Collagen-binding mode of vWF-A3 domain determined by a transferred cross-saturation experiment.
  Nat Struct Biol, 10, 53-58.  
12806635 R.I.Handin (2003).
A hitchhiker's guide to the galaxy--an H. pylori travel guide.
  Gastroenterology, 124, 1983-1985.  
12871266 Z.M.Ruggeri (2003).
Von Willebrand factor, platelets and endothelial cell interactions.
  J Thromb Haemost, 1, 1335-1342.  
11756664 B.Savage, J.J.Sixma, and Z.M.Ruggeri (2002).
Functional self-association of von Willebrand factor during platelet adhesion under flow.
  Proc Natl Acad Sci U S A, 99, 425-430.  
12388743 C.A.Whittaker, and R.O.Hynes (2002).
Distribution and evolution of von Willebrand/integrin A domains: widely dispersed domains with roles in cell adhesion and elsewhere.
  Mol Biol Cell, 13, 3369-3387.  
  11876085 D.E.Gullberg, and E.Lundgren-Akerlund (2002).
Collagen-binding I domain integrins--what do they do?
  Prog Histochem Cytochem, 37, 3.  
  12102729 J.E.Garbarino, and I.R.Gibbons (2002).
Expression and genomic analysis of midasin, a novel and highly conserved AAA protein distantly related to dynein.
  BMC Genomics, 3, 18.  
11468390 E.G.Huizinga, A.Schouten, T.M.Connolly, J.Kroon, J.J.Sixma, and P.Gros (2001).
The structure of leech anti-platelet protein, an inhibitor of haemostasis.
  Acta Crystallogr D Biol Crystallogr, 57, 1071-1078.
PDB code: 1i8n
10805782 J.R.Huth, E.T.Olejniczak, R.Mendoza, H.Liang, E.A.Harris, M.L.Lupher, A.E.Wilson, S.W.Fesik, and D.E.Staunton (2000).
NMR and mutagenesis evidence for an I domain allosteric site that regulates lymphocyte function-associated antigen 1 ligand binding.
  Proc Natl Acad Sci U S A, 97, 5231-5236.  
10520599 Z.Li (1999).
The alphaMbeta2 integrin and its role in neutrophil function.
  Cell Res, 9, 171-178.  
  9687375 E.T.Baldwin, R.W.Sarver, G.L.Bryant, K.A.Curry, M.B.Fairbanks, B.C.Finzel, R.L.Garlick, R.L.Heinrikson, N.C.Horton, L.L.Kelley, A.M.Mildner, J.B.Moon, J.E.Mott, V.T.Mutchler, C.S.Tomich, K.D.Watenpaugh, and V.H.Wiley (1998).
Cation binding to the integrin CD11b I domain and activation model assessment.
  Structure, 6, 923-935.
PDB codes: 1bho 1bhq 1idn
9759493 J.E.Sadler (1998).
Biochemistry and genetics of von Willebrand factor.
  Annu Rev Biochem, 67, 395-424.  
9501911 R.Celikel, K.I.Varughese, Madhusudan, A.Yoshioka, J.Ware, Z.M.Ruggeri, R.Celikel, K.I.Varughese, Madhusudan, A.Yoshioka, J.Ware, and Z.M.Ruggeri (1998).
Crystal structure of the von Willebrand factor A1 domain in complex with the function blocking NMC-4 Fab.
  Nat Struct Biol, 5, 189-194.
PDB code: 1oak
9501084 T.Sasaki, E.Hohenester, W.Göhring, and R.Timpl (1998).
Crystal structure and mapping by site-directed mutagenesis of the collagen-binding epitope of an activated form of BM-40/SPARC/osteonectin.
  EMBO J, 17, 1625-1634.
PDB code: 1nub
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.