1tle: Difference between revisions
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[[Image:1tle. | [[Image:1tle.jpg|left|200px]]<br /><applet load="1tle" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1tle" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1tle" /> | caption="1tle" /> | ||
'''LE (LAMININ-TYPE EGF-LIKE) MODULE GIII4 IN SOLUTION AT PH 3.5 AND 290 K, NMR, 14 STRUCTURES'''<br /> | '''LE (LAMININ-TYPE EGF-LIKE) MODULE GIII4 IN SOLUTION AT PH 3.5 AND 290 K, NMR, 14 STRUCTURES'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
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]. | 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]. Known structural/functional Site: <scene name='pdbsite=BIN:Binding Site To Nidogen'>BIN</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TLE OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: nidogen binding]] | [[Category: nidogen binding]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:02:07 2007'' | ||
Revision as of 18:52, 18 December 2007
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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, 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.
About this StructureAbout this Structure
1TLE is a Single protein structure of sequence from Mus musculus. Known structural/functional Site: . 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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