spacer
spacer

PDBsum entry 1buu
Go to PDB code: 
protein metals links
Sugar binding protein PDB id
1buu

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chain
149 a.a. *
Metals
_HO
Waters ×171
* Residue conservation analysis
PDB id:
1buu
Name: Sugar binding protein
Title: One ho3+ form of rat mannose-binding protein a
Structure: Protein (mannose-binding protein a). Chain: a. Fragment: lectin, trimerization, and portion of collagenous domain domains. Engineered: yes
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Organ: liver. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Trimer (from PDB file)
Resolution:
1.90Å     R-factor:   0.198     R-free:   0.214
Authors: K.K.-S.Ng,S.Park-Snyder,W.I.Weis
Key ref:
K.K.Ng et al. (1998). Ca2+-dependent structural changes in C-type mannose-binding proteins. Biochemistry, 37, 17965-17976. PubMed id: 9922165 DOI: 10.1021/bi981972a
Date:
06-Sep-98     Release date:   09-Sep-98    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P19999  (MBL1_RAT) -  Mannose-binding protein A from Rattus norvegicus
Seq:
Struc: 		238 a.a.
149 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1021/bi981972a Biochemistry 37:17965-17976 (1998)
PubMed id: 9922165  
 
 
Ca2+-dependent structural changes in C-type mannose-binding proteins.
K.K.Ng, S.Park-Snyder, W.I.Weis.
 
  ABSTRACT  
 
C-type animal lectins are a diverse family of proteins which mediate cell-surface carbohydrate-recognition events through a conserved carbohydrate-recognition domain (CRD). Most members of this family possess a carbohydrate-binding activity that depends strictly on the binding of Ca2+ at two sites, designated 1 and 2, in the CRD. The structural transitions associated with Ca2+ binding in C-type lectins have been investigated by determining high-resolution crystal structures of rat serum mannose-binding protein (MBP) bound to one Ho3+ in place of Ca2+, and the apo form of rat liver MBP. The removal of Ca2+ does not affect the core structure of the CRD, but dramatic conformational changes occur in the loops. The most significant structural change in the absence of Ca2+ is the isomerization of a cis-peptide bond preceding a conserved proline residue in Ca2+ site 2. This bond adopts the cis conformation in all Ca2+-bound structures, whereas both cis and trans conformations are observed in the absence of Ca2+. The pattern of structural changes in the three loops that interact with Ca2+ is dictated in large part by the conformation of the prolyl peptide bond. The highly conserved nature of Ca2+ site 2 suggests that the transitions observed in MBPs are general features of Ca2+ binding in C-type lectins.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20676430 B.Apostolovic, M.Danial, and H.A.Klok (2010).
Coiled coils: attractive protein folding motifs for the fabrication of self-assembled, responsive and bioactive materials.
  Chem Soc Rev, 39, 3541-3575.  
20382864 R.E.Lehotzky, C.L.Partch, S.Mukherjee, H.L.Cash, W.E.Goldman, K.H.Gardner, and L.V.Hooper (2010).
Molecular basis for peptidoglycan recognition by a bactericidal lectin.
  Proc Natl Acad Sci U S A, 107, 7722-7727.  
17420244 H.Feinberg, M.E.Taylor, and W.I.Weis (2007).
Scavenger receptor C-type lectin binds to the leukocyte cell surface glycan Lewis(x) by a novel mechanism.
  J Biol Chem, 282, 17250-17258.
PDB codes: 2ox8 2ox9
16765898 B.A.Wurzburg, S.S.Tarchevskaya, and T.S.Jardetzky (2006).
Structural changes in the lectin domain of CD23, the low-affinity IgE receptor, upon calcium binding.
  Structure, 14, 1049-1058.
PDB codes: 2h2r 2h2t
16765887 P.D.Sun (2006).
Human CD23: is it a lectin in disguise?
  Structure, 14, 950-951.  
16336259 A.N.Zelensky, and J.E.Gready (2005).
The C-type lectin-like domain superfamily.
  FEBS J, 272, 6179-6217.  
15609336 S.Lorenzen, B.Peters, A.Goede, R.Preissner, and C.Frömmel (2005).
Conservation of cis prolyl bonds in proteins during evolution.
  Proteins, 58, 589-595.  
15030473 J.K.van de Wetering, L.M.van Golde, and J.J.Batenburg (2004).
Collectins: players of the innate immune system.
  Eur J Biochem, 271, 1229-1249.  
14970226 S.V.Su, P.Hong, S.Baik, O.A.Negrete, K.B.Gurney, and B.Lee (2004).
DC-SIGN binds to HIV-1 glycoprotein 120 in a distinct but overlapping fashion compared with ICAM-2 and ICAM-3.
  J Biol Chem, 279, 19122-19132.  
12743029 H.Feinberg, J.C.Uitdehaag, J.M.Davies, R.Wallis, K.Drickamer, and W.I.Weis (2003).
Crystal structure of the CUB1-EGF-CUB2 region of mannose-binding protein associated serine protease-2.
  EMBO J, 22, 2348-2359.
PDB code: 1nt0
12913002 J.F.Head, T.R.Mealy, F.X.McCormack, and B.A.Seaton (2003).
Crystal structure of trimeric carbohydrate recognition and neck domains of surfactant protein A.
  J Biol Chem, 278, 43254-43260.
PDB codes: 1r13 1r14
11918697 C.Galustian, R.A.Childs, M.Stoll, H.Ishida, M.Kiso, and T.Feizi (2002).
Synergistic interactions of the two classes of ligand, sialyl-Lewis(a/x) fuco-oligosaccharides and short sulpho-motifs, with the P- and L-selectins: implications for therapeutic inhibitor designs.
  Immunology, 105, 350-359.  
10679456 C.Schiene, and G.Fischer (2000).
Enzymes that catalyse the restructuring of proteins.
  Curr Opin Struct Biol, 10, 40-45.  
  11045608 K.Håkansson, and K.B.Reid (2000).
Collectin structure: a review.
  Protein Sci, 9, 1607-1617.  
10508765 K.Drickamer (1999).
C-type lectin-like domains.
  Curr Opin Struct Biol, 9, 585-590.  
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 codes are shown on the right.

 

spacer
spacer