PDBsum entry 1uvg

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Serine proteinase inhibitor PDB id
Protein chain
76 a.a. *
* Residue conservation analysis
PDB id:
Name: Serine proteinase inhibitor
Title: Solution structure of the 15th domain of lekti
Structure: Serine proteinase inhibitor kazal type 5. Chain: a. Fragment: lekti-domain15, residues 989-1064. Synonym: lympho-epithelial, kazal-type related inhibitor, lekti. Engineered: yes. Other_details: disulphide bonds between cys5 and cys40, between cys18 and cys37, between cys26 and cys58
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: vaginal epithel. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_variant: de3.
NMR struc: 31 models
Authors: K.Vitzithum,P.Roesch,U.C.Marx
Key ref:
H.Tidow et al. (2004). The solution structure of a chimeric LEKTI domain reveals a chameleon sequence. Biochemistry, 43, 11238-11247. PubMed id: 15366933 DOI: 10.1021/bi0492399
20-Jan-04     Release date:   14-Apr-05    
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Protein chain
Pfam   ArchSchema ?
Q9NQ38  (ISK5_HUMAN) -  Serine protease inhibitor Kazal-type 5
1064 a.a.
76 a.a.
Key:    PfamA domain  Secondary structure  CATH domain


DOI no: 10.1021/bi0492399 Biochemistry 43:11238-11247 (2004)
PubMed id: 15366933  
The solution structure of a chimeric LEKTI domain reveals a chameleon sequence.
H.Tidow, T.Lauber, K.Vitzithum, C.P.Sommerhoff, P.Rösch, U.C.Marx.
The conversion of an alpha-helical to a beta-strand conformation and the presence of chameleon sequences are fascinating from the perspective that such structural features are implicated in the induction of amyloid-related fatal diseases. In this study, we have determined the solution structure of a chimeric domain (Dom1PI) from the multidomain Kazal-type serine proteinase inhibitor LEKTI using multidimensional NMR spectroscopy. This chimeric protein was constructed to investigate the reasons for differences in the folds of the homologous LEKTI domains 1 and 6 [Lauber, T., et al. (2003) J. Mol. Biol. 328, 205-219]. In Dom1PI, two adjacent phenylalanine residues (F28 and F29) of domain 1 were substituted with proline and isoleucine, respectively, as found in the corresponding P4' and P5' positions of domain 6. The three-dimensional structure of Dom1PI is significantly different from the structure of domain 1 and closely resembles the structure of domain 6, despite the sequence being identical to that of domain 1 except for the two substituted phenylalanine residues and being only 31% identical to the sequence of domain 6. The mutation converted a short 3(10)-helix into an extended loop conformation and parts of the long COOH-terminal alpha-helix of domain 1 into a beta-hairpin structure. The latter conformational change occurs in a sequence stretch distinct from the region containing the substituted residues. Therefore, this switch from an alpha-helical structure to a beta-hairpin structure indicates a chameleon sequence of seven residues. We conclude that the secondary structure of Dom1PI is determined not only by the local protein sequence but also by nonlocal interactions.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20969427 A.M.Ruvinsky, and I.A.Vakser (2010).
Sequence composition and environment effects on residue fluctuations in protein structures.
  J Chem Phys, 133, 155101.  
20955581 N.Bhattacharjee, and P.Biswas (2010).
Statistical analysis and molecular dynamics simulations of ambivalent α-helices.
  BMC Bioinformatics, 11, 519.  
18287054 A.R.Davidson (2008).
A folding space odyssey.
  Proc Natl Acad Sci U S A, 105, 2759-2760.  
17434131 G.A.Belogurov, M.N.Vassylyeva, V.Svetlov, S.Klyuyev, N.V.Grishin, D.G.Vassylyev, and I.Artsimovitch (2007).
Structural basis for converting a general transcription factor into an operon-specific virulence regulator.
  Mol Cell, 26, 117-129.
PDB code: 2oug
17299764 J.T.Guo, J.W.Jaromczyk, and Y.Xu (2007).
Analysis of chameleon sequences and their implications in biological processes.
  Proteins, 67, 548-558.  
17240325 T.O.Yeates (2007).
Protein structure: evolutionary bridges to new folds.
  Curr Biol, 17, R48-R50.  
16650981 A.Andreeva, and A.G.Murzin (2006).
Evolution of protein fold in the presence of functional constraints.
  Curr Opin Struct Biol, 16, 399-408.  
16307483 N.M.Schechter, E.J.Choi, Z.M.Wang, Y.Hanakawa, J.R.Stanley, Y.Kang, G.L.Clayman, and A.Jayakumar (2005).
Inhibition of human kallikreins 5 and 7 by the serine protease inhibitor lympho-epithelial Kazal-type inhibitor (LEKTI).
  Biol Chem, 386, 1173-1184.  
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