1tle: Difference between revisions

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, C-terminal segment has an S-like backbone profile with a crossover at the, last disulfide bridge and comprises two three-residue long beta-strands, that form an antiparallel beta-sheet. The LE module possesses an exposed, nidogen binding loop that projects away from the main body of the protein., The side-chains of three amino acids which are crucial for binding (Asp, Asn, Val) are all exposed at the domain surface. An inactivating Asn-Ser, mutation in this region showed the same 3D structure indicating that these, three residues, and possibly an additional Tyr in an adjacent loop, provide direct contacts in the interaction with nidogen.

1TLE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Structure known Active Site: BIN. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TLE OCA].  

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