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PDBsum entry 1tkn

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protein links
Membrane protein PDB id
1tkn
Jmol
Contents
Protein chain
110 a.a. *
* Residue conservation analysis
PDB id:
1tkn
Name: Membrane protein
Title: Solution structure of cappd , An independently folded extracellular domain of human amyloid-beta precursor protein
Structure: Amyloid beta a4 protein. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: app, a4, ad1. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
NMR struc: 20 models
Authors: I.Dulubova,A.Ho,I.Huryeva,T.C.Sudhof,J.Rizo
Key ref:
I.Dulubova et al. (2004). Three-dimensional structure of an independently folded extracellular domain of human amyloid-beta precursor protein. Biochemistry, 43, 9583-9588. PubMed id: 15274612 DOI: 10.1021/bi049041o
Date:
08-Jun-04     Release date:   03-Aug-04    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P05067  (A4_HUMAN) -  Amyloid beta A4 protein
Seq:
Struc:
 
Seq:
Struc:
770 a.a.
110 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     nervous system development   1 term 

 

 
DOI no: 10.1021/bi049041o Biochemistry 43:9583-9588 (2004)
PubMed id: 15274612  
 
 
Three-dimensional structure of an independently folded extracellular domain of human amyloid-beta precursor protein.
I.Dulubova, A.Ho, I.Huryeva, T.C.Südhof, J.Rizo.
 
  ABSTRACT  
 
Cleavage of amyloid-beta precursor protein (APP) by site-specific proteases generates amyloid-beta peptides (Abetas), which are thought to induce Alzheimer's disease. We have identified an independently folded extracellular domain of human APP localized proximal to the Abeta sequence, and determined the three-dimensional structure of this domain by NMR spectroscopy. The domain is composed of four alpha-helices, three of which form a tight antiparallel bundle, and constitutes the C-terminal half of the central extracellular region of APP that has been implicated in the regulation of APP cleavage. Sequence comparisons demonstrate that the domain is highly conserved among all members of the APP family, including invertebrate homologues, suggesting an important role for this region in the biological function of APP. The identification of this domain and the availability of its atomic structure will facilitate analysis of APP function and of the role of the extracellular region in the regulation of APP cleavage.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19906646 J.T.Hoopes, X.Liu, X.Xu, B.Demeler, E.Folta-Stogniew, C.Li, and Y.Ha (2010).
Structural characterization of the E2 domain of APL-1, a Caenorhabditis elegans homolog of human amyloid precursor protein, and its heparin binding site.
  J Biol Chem, 285, 2165-2173.
PDB codes: 3k66 3k6b
20212142 S.O.Dahms, S.Hoefgen, D.Roeser, B.Schlott, K.H.Gührs, and M.E.Than (2010).
Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein.
  Proc Natl Acad Sci U S A, 107, 5381-5386.
PDB code: 3ktm
19336403 M.Gralle, M.G.Botelho, and F.S.Wouters (2009).
Neuroprotective secreted amyloid precursor protein acts by disrupting amyloid precursor protein dimers.
  J Biol Chem, 284, 15016-15025.  
18702528 A.J.Beel, C.K.Mobley, H.J.Kim, F.Tian, A.Hadziselimovic, B.Jap, J.H.Prestegard, and C.R.Sanders (2008).
Structural studies of the transmembrane C-terminal domain of the amyloid precursor protein (APP): does APP function as a cholesterol sensor?
  Biochemistry, 47, 9428-9446.  
18182389 D.Kaden, L.M.Munter, M.Joshi, C.Treiber, C.Weise, T.Bethge, P.Voigt, M.Schaefer, M.Beyermann, B.Reif, and G.Multhaup (2008).
Homophilic interactions of the amyloid precursor protein (APP) ectodomain are regulated by the loop region and affect beta-secretase cleavage of APP.
  J Biol Chem, 283, 7271-7279.  
17267616 A.Hornsten, J.Lieberthal, S.Fadia, R.Malins, L.Ha, X.Xu, I.Daigle, M.Markowitz, G.O'Connor, R.Plasterk, and C.Li (2007).
APL-1, a Caenorhabditis elegans protein related to the human beta-amyloid precursor protein, is essential for viability.
  Proc Natl Acad Sci U S A, 104, 1971-1976.  
17428603 M.Gralle, and S.T.Ferreira (2007).
Structure and functions of the human amyloid precursor protein: the whole is more than the sum of its parts.
  Prog Neurobiol, 82, 11-32.  
16805778 C.L.Masters, R.Cappai, K.J.Barnham, and V.L.Villemagne (2006).
Molecular mechanisms for Alzheimer's disease: implications for neuroimaging and therapeutics.
  J Neurochem, 97, 1700-1725.  
16252002 C.Reinhard, S.S.Hébert, and B.De Strooper (2005).
The amyloid-beta precursor protein: integrating structure with biological function.
  EMBO J, 24, 3996-4006.  
15815985 K.S.Rotondi, and L.M.Gierasch (2005).
A well-defined amphipathic conformation for the calcium-free cyclic lipopeptide antibiotic, daptomycin, in aqueous solution.
  Biopolymers, 80, 374-385.  
15465814 C.Treiber, A.Simons, M.Strauss, M.Hafner, R.Cappai, T.A.Bayer, and G.Multhaup (2004).
Clioquinol mediates copper uptake and counteracts copper efflux activities of the amyloid precursor protein of Alzheimer's disease.
  J Biol Chem, 279, 51958-51964.  
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.