1tle
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LE (LAMININ-TYPE EGF-LIKE) MODULE GIII4 IN SOLUTION AT PH 3.5 AND 290 K, NMR, 14 STRUCTURES
OverviewOverview
The structure of the single LE module between residues 791 and 848 of the, laminin gamma1 chain, which contains the high affinity binding site for, nidogen, has been probed using NMR methods. The module folds into an, autonomous domain which has a stable and unique three-dimensional (3D), structure in solution. The 3D structure was determined on the basis of 362, interproton distance constraints derived from nuclear Overhauser, enhancement measurements and 39 phi angles, supplemented by 5 psi and 22, chi1 angles. The main features of the NMR structures are two-stranded, antiparallel beta-sheets which are separated by loops and cross-connected, by four disulfide bridges. The N-terminal segment which contains the first, three disulfide bridges is similar to epidermal growth factor. The, ... [(full description)]
About this StructureAbout this Structure
1TLE is a [Single protein] structure of sequence from [Mus musculus]. Full crystallographic information is available from [OCA].
ReferenceReference
Structure of the nidogen binding LE module of the laminin gamma1 chain in solution., Baumgartner R, Czisch M, Mayer U, Poschl E, Huber R, Timpl R, Holak TA, J Mol Biol. 1996 Apr 5;257(3):658-68. PMID:8648631
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