1tle: Difference between revisions
New page: left|200px<br /> <applet load="1tle" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tle" /> '''LE (LAMININ-TYPE EGF-LIKE) MODULE GIII4 IN ... |
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== | ==LE (LAMININ-TYPE EGF-LIKE) MODULE GIII4 IN SOLUTION AT PH 3.5 AND 290 K, NMR, 14 STRUCTURES== | ||
The structure of the single LE module between residues 791 and 848 of the | <StructureSection load='1tle' size='340' side='right'caption='[[1tle]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1tle]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TLE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TLE FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 14 models</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tle OCA], [https://pdbe.org/1tle PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tle RCSB], [https://www.ebi.ac.uk/pdbsum/1tle PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tle ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/LAMC1_MOUSE LAMC1_MOUSE] Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tl/1tle_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1tle ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:8648631</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1tle" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Laminin|Laminin]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Baumgartner R]] | |||
[[Category: Baumgartner | [[Category: Czisch M]] | ||
[[Category: Czisch | [[Category: Holak TA]] | ||
[[Category: Holak | [[Category: Huber R]] | ||
[[Category: Huber | [[Category: Mayer U]] | ||
[[Category: Mayer | [[Category: Schl EP]] | ||
[[Category: Schl | [[Category: Timpl R]] | ||
[[Category: Timpl | |||
