PDBsum entry 2l3h

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protein links
Hydrolase PDB id
Protein chain
39 a.a.
PDB id:
Name: Hydrolase
Title: Nmr structure in a membrane environment reveals putative amy regions of the sevi precursor peptide pap248-286
Structure: Prostatic acid phosphatase. Chain: a. Fragment: unp residues 248-286. Engineered: yes
Source: Synthetic: yes. Homo sapiens. Human. Organism_taxid: 9606. Other_details: acpp
NMR struc: 8 models
Authors: A.Ramamoorthy,R.Nanga,J.Brender,S.Vivekanandan,N.Popovych
Key ref: R.P.Nanga et al. (2009). NMR structure in a membrane environment reveals putative amyloidogenic regions of the SEVI precursor peptide PAP(248-286). J Am Chem Soc, 131, 17972-17979. PubMed id: 19995078
13-Sep-10     Release date:   06-Oct-10    
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Protein chain
Pfam   ArchSchema ?
P15309  (PPAP_HUMAN) -  Prostatic acid phosphatase
386 a.a.
39 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class 1: E.C.  - Acid phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: A phosphate monoester + H2O = an alcohol + phosphate
phosphate monoester
+ H(2)O
= alcohol
+ phosphate
   Enzyme class 2: E.C.  - 5'-nucleotidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
+ H(2)O
= ribonucleoside
+ phosphate
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site


J Am Chem Soc 131:17972-17979 (2009)
PubMed id: 19995078  
NMR structure in a membrane environment reveals putative amyloidogenic regions of the SEVI precursor peptide PAP(248-286).
R.P.Nanga, J.R.Brender, S.Vivekanandan, N.Popovych, A.Ramamoorthy.
Semen is the main vector for HIV transmission worldwide. Recently, a peptide fragment (PAP(248-286)) has been isolated from seminal fluid that dramatically enhances HIV infectivity by up to 4-5 orders of magnitude. PAP(248-286) appears to enhance HIV infection by forming amyloid fibers known as SEVI, which are believed to enhance the attachment of the virus by bridging interactions between virion and host-cell membranes. We have solved the atomic-level resolution structure of the SEVI precursor PAP(248-286) using NMR spectroscopy in SDS micelles, which serve as a model membrane system. PAP(248-286), which does not disrupt membranes like most amyloid proteins, binds superficially to the surface of the micelle, in contrast to other membrane-disruptive amyloid peptides that generally penetrate into the core of the membrane. The structure of PAP(248-286) is unlike most amyloid peptides in that PAP(248-286) is mostly disordered when bound to the surface of the micelle, as opposed to the alpha-helical structures typically found of most amyloid proteins. The highly disordered nature of the SEVI peptide may explain the unique ability of SEVI amyloid fibers to enhance HIV infection as partially disordered amyloid fibers will have a greater capture radius for the virus than compact amyloid fibers. Two regions of nascent structure (an alpha-helix from V262-H270 and a dynamic alpha/3(10) helix from S279-L283) match the prediction of highly amyloidogenic sequences and may serve as nuclei for aggregation and amyloid fibril formation. The structure presented here can be used for the rational design of mutagenesis studies on SEVI amyloid formation and viral infection enhancement.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21219138 R.Tycko (2011).
Solid-state NMR studies of amyloid fibril structure.
  Annu Rev Phys Chem, 62, 279-299.  
20936218 G.Hou, S.Paramasivam, I.J.Byeon, A.M.Gronenborn, and T.Polenova (2010).
Determination of relative tensor orientations by γ-encoded chemical shift anisotropy/heteronuclear dipolar coupling 3D NMR spectroscopy in biological solids.
  Phys Chem Chem Phys, 12, 14873-14883.  
  20573198 K.A.Kim, M.Yolamanova, O.Zirafi, N.R.Roan, L.Standker, W.G.Forssmann, A.Burgener, N.Dejucq-Rainsford, B.H.Hahn, G.M.Shaw, W.C.Greene, F.Kirchhoff, and J.Muench (2010).
Semen-mediated enhancement of HIV infection is donor-dependent and correlates with the levels of SEVI.
  Retrovirology, 7, 55.  
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