2dox | pdb_00002dox

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

THAUMATIN-LIKE PROTEIN 4

spinqualitylabelsall models 2dox Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed Barley plants are known to produce various PR-5 proteins. Transcripts encoding eight different barley PR-5 proteins (TLPs 1-8, TLP for thaumatin-like protein) were identified and cloned - seven from infected leaves and one from developing grains. Here, we describe the cDNA sequences of four of these TLP isoforms. Moreover, the TLPs from the infected leaves (TLPs 1, 2, and TLPs 4-8) were subjected to MALDI-TOF mass spectrometric measurements that resulted in protein fragments consistent with their deduced peptide sequences. Multiple sequence alignment analysis revealed that the TLPs in barley fall into two groups: long-chain proteins (TLPs 5-8) having 16 cysteine residues and short-chain proteins (TLPs 1-4) with only 10 cysteine residues. Finally, modelling experiments highlighted the effects of sequence differences between the TLP isoforms in terms of their secondary structures and their molecular electrostatic potentials. We propose that these sequence differences have implications for the target preferences of the different isomers. cDNA sequences, MALDI-TOF analyses, and molecular modelling of barley PR-5 proteins.,Reiss E, Schlesier B, Brandt W Phytochemistry. 2006 Sep;67(17):1856-64. Epub 2006 Jul 31. PMID:16876835 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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