This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1tle

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 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 ...)
Current revision (08:42, 1 May 2024) (edit) (undo)
 
(21 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1tle.gif|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 SOLUTION AT PH 3.5 AND 290 K, NMR, 14 STRUCTURES'''<br />
 
-
==Overview==
+
==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, 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, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?8648631 (full description)]]
+
<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</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/initialview01.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>
-
==About this Structure==
+
==See Also==
-
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]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TLE OCA]].
+
*[[Laminin|Laminin]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8648631 8648631]
+
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
-
[[Category: Single protein]]
+
[[Category: Baumgartner R]]
-
[[Category: Baumgartner, R.]]
+
[[Category: Czisch M]]
-
[[Category: Czisch, M.]]
+
[[Category: Holak TA]]
-
[[Category: Holak, T.A.]]
+
[[Category: Huber R]]
-
[[Category: Huber, R.]]
+
[[Category: Mayer U]]
-
[[Category: Mayer, U.]]
+
[[Category: Schl EP]]
-
[[Category: Schl, E.P.]]
+
[[Category: Timpl R]]
-
[[Category: Timpl, R.]]
+
-
[[Category: extracellular matrix protein]]
+
-
[[Category: glycoprotein]]
+
-
[[Category: le-module]]
+
-
[[Category: nidogen binding]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 17:16:24 2007''
+

Current revision

LE (LAMININ-TYPE EGF-LIKE) MODULE GIII4 IN SOLUTION AT PH 3.5 AND 290 K, NMR, 14 STRUCTURES

PDB ID 1tle

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools