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PDBsum entry 1pmc

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Proteinase inhibitor PDB id
1pmc

 

 

 

 

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Contents
Protein chain
36 a.a.
PDB id:
1pmc
Name: Proteinase inhibitor
Title: Proteinase inhibitor pmp-c (nmr, 36 structures)
Structure: Proteinase inhibitor pmp-c. Chain: a. Synonym: lmci ii. Engineered: yes
Source: Locusta migratoria. Migratory locust. Organism_taxid: 7004. Organ: brain. Tissue: hemolymph and fat body
NMR struc: 36 models
Authors: G.Mer,H.Hietter,J.-F.Lefevre
Key ref: G.Mer et al. (1996). Solution structure of PMP-C: a new fold in the group of small serine proteinase inhibitors. J Mol Biol, 258, 158-171. PubMed id: 8613985
Date:
17-Sep-95     Release date:   29-Jan-96    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P80060  (LCM_LOCMI) -  Protease inhibitors from Locusta migratoria
Seq:
Struc:
92 a.a.
36 a.a.
Key:    PfamA domain  Secondary structure

 

 
J Mol Biol 258:158-171 (1996)
PubMed id: 8613985  
 
 
Solution structure of PMP-C: a new fold in the group of small serine proteinase inhibitors.
G.Mer, H.Hietter, C.Kellenberger, M.Renatus, B.Luu, J.F.Lefèvre.
 
  ABSTRACT  
 
The solution structure and the disulfide pairings of a 36-residue proteinase inhibitor isolated from the insect Locusta migratoria have been determined using NMR spectroscopy and simulated annealing calculations. The peptide, termed PMP-C, was previously shown to inhibit bovine alpha-chymotrypsin as well as human leukocyte elastase, and was also found to block high-voltage-activated Ca2+ currents in rat sensory neurones. PMP-C has a prolate ellipsoid shape and adopts a tertiary fold hitherto unobserved in the large group of small "canonical" proteinase inhibitors. The over-all fold consists mainly of three strands arranged in a right-handed twisted, antiparallel, beta-sheet that demarcates a cavity, together with a linear amino-terminal segment oriented almost perpendicular to the three strands of the beta-sheet. Inside the cavity a phenyl ring constitutes the centre of a hydrophobic core. The proteinase binding loop is located in the carboxy-terminal part of the molecule, between two cysteine residues involved in disulfide bridges. Its conformation resembles that found in other small canonical proteinase inhibitors. A comparison of PMP-C structure with the recently published solution structure of the related peptide PMP-D2 shows that the most significant differences are complementary changes involved in the stabilization of similar folds. This comparison led us to review the structure of PMP-D2 and to identify two salt bridges in PMP-D2.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19435517 B.Breugelmans, G.Simonet, V.van Hoef, S.Van Soest, and J.Vanden Broeck (2009).
Identification, distribution and molecular evolution of the pacifastin gene family in Metazoa.
  BMC Evol Biol, 9, 97.  
18353103 B.Breugelmans, G.Simonet, V.van Hoef, I.Claeys, S.Van Soest, and J.Vanden Broeck (2008).
Quantitative RT-PCR analysis of pacifastin-related precursor transcripts during the reproductive cycle of solitarious and gregarious desert locusts.
  Insect Mol Biol, 17, 137-145.  
19020355 P.Leone, A.Roussel, and C.Kellenberger (2008).
Structure of Locusta migratoria protease inhibitor 3 (LMPI-3) in complex with Fusarium oxysporum trypsin.
  Acta Crystallogr D Biol Crystallogr, 64, 1165-1171.
PDB code: 2vu8
  16820690 S.Roy, P.Aravind, C.Madhurantakam, A.K.Ghosh, R.Sankaranarayanan, and A.K.Das (2006).
Crystallization and preliminary X-ray diffraction analysis of a protease inhibitor from the haemolymph of the Indian tasar silkworm Antheraea mylitta.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 669-671.  
16623717 Z.Gáspári, B.Szenthe, A.Patthy, W.M.Westler, L.Gráf, and A.Perczel (2006).
Local binding with globally distributed changes in a small protease inhibitor upon enzyme binding.
  FEBS J, 273, 1831-1842.  
12919325 S.F.Foley, H.W.van Vlijmen, R.E.Boynton, H.B.Adkins, A.E.Cheung, J.Singh, M.Sanicola, C.N.Young, and D.Wen (2003).
The CRIPTO/FRL-1/CRYPTIC (CFC) domain of human Cripto. Functional and structural insights through disulfide structure analysis.
  Eur J Biochem, 270, 3610-3618.  
11933060 H.Hegyi, J.Lin, D.Greenbaum, and M.Gerstein (2002).
Structural genomics analysis: characteristics of atypical, common, and horizontally transferred folds.
  Proteins, 47, 126-141.  
12036964 V.M.Panin, L.Shao, L.Lei, D.J.Moloney, K.D.Irvine, and R.S.Haltiwanger (2002).
Notch ligands are substrates for protein O-fucosyltransferase-1 and Fringe.
  J Biol Chem, 277, 29945-29952.  
11856311 Z.Gáspári, A.Patthy, L.Gráf, and A.Perczel (2002).
Comparative structure analysis of proteinase inhibitors from the desert locust, Schistocerca gregaria.
  Eur J Biochem, 269, 527-537.
PDB codes: 1kgm 1kio 1kj0
11495915 A.Roussel, M.Mathieu, A.Dobbs, B.Luu, C.Cambillau, and C.Kellenberger (2001).
Complexation of two proteic insect inhibitors to the active site of chymotrypsin suggests decoupled roles for binding and selectivity.
  J Biol Chem, 276, 38893-38898.
PDB codes: 1gl0 1gl1
10556568 Z.Malik, S.Amir, G.Pál, Z.Buzás, E.Várallyay, J.Antal, Z.Szilágyi, K.Vékey, B.Asbóth, A.Patthy, and L.Gráf (1999).
Proteinase inhibitors from desert locust, Schistocerca gregaria: engineering of both P(1) and P(1)' residues converts a potent chymotrypsin inhibitor to a potent trypsin inhibitor.
  Biochim Biophys Acta, 1434, 143-150.  
9032075 P.Holliger, and L.Riechmann (1997).
A conserved infection pathway for filamentous bacteriophages is suggested by the structure of the membrane penetration domain of the minor coat protein g3p from phage fd.
  Structure, 5, 265-275.
PDB code: 1fgp
9144657 R.H.Scott, V.J.Gorton, L.Harding, D.Patel, S.Pacey, C.Kellenberger, H.Hietter, and I.Bermudez (1997).
Inhibition of neuronal high voltage-activated calcium channels by insect peptides: a comparison with the actions of omega-conotoxin GVIA.
  Neuropharmacology, 36, 195-208.  
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.

 

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