1n5p

Solution structure of the cathelin-like domain of protegrins (all amide bonds involving proline residues are in trans conformation)

spinqualitylabelsall models 1n5p Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1n5p is a 1 chain structure with sequence from Sus scrofa. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 15 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PG4_PIG Microbicidal activity (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed In mammals, numerous precursors of antibacterial peptides with unrelated sequences share a similar prosequence of 94-114 residues, termed the cathelin-like domain. The cathelin-like domain of protegrin-3 (ProS) was overexpressed in Escherichia coli and uniformly labeled with (15)N or (15)N and (13)C, and its three-dimensional structure was determined by heteronuclear NMR at pH 6.2. Under these conditions and due to the cis-trans isomerization of the R(87)-P(88) and D(118)-P(119) amide bonds, the ProS structure was found to adopt four almost equally populated conformations in slow exchange on the NMR chemical shift time scale. The ProS structure consists of an N-terminal alpha-helix (Y(34)-N(48)) cradled by a four-stranded antiparallel beta-sheet (beta1, N(53)-L(60); beta2, K(74)-P(86); beta3, V(104)-V(111); and beta4, I(122)-C(124)). The solution structure of ProS, which is monomeric, allowed us to determine the structure of the L1 and L2 loops, which are too mobile in the crystal structure. The regions common to the solution and X-ray structures were found to be very similar. Finally, since the overall fold of ProS is very similar to that of cystatins despite a low degree of sequence identity, the ProS solution structure was compared to the solution and X-ray structures of the chicken cystatin. This comparison revealed that the structures of the L1 and L2 loops as well as that of the appending domain are quite different in the two proteins. These differences are mainly due to the high proline residue content (10%) which disorganizes the hydrogen bond network of a part of the ProS beta-sheet in contrast to that of the chicken cystatin structure. NMR structure of the cathelin-like domain of the protegrin-3 precursor.,Yang Y, Sanchez JF, Strub MP, Brutscher B, Aumelas A Biochemistry. 2003 Apr 29;42(16):4669-80. PMID:12705830 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Protegrin

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