1tle

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1tle.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1tle.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1tle| PDB=1tle | SCENE= }}
{{STRUCTURE_1tle| PDB=1tle | SCENE= }}
-
'''LE (LAMININ-TYPE EGF-LIKE) MODULE GIII4 IN SOLUTION AT PH 3.5 AND 290 K, NMR, 14 STRUCTURES'''
+
===LE (LAMININ-TYPE EGF-LIKE) MODULE GIII4 IN SOLUTION AT PH 3.5 AND 290 K, NMR, 14 STRUCTURES===
-
==Overview==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8648631}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8648631 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8648631}}
==About this Structure==
==About this Structure==
-
1TLE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TLE OCA].
+
1TLE is a [[Single protein]] structure of sequence from [http://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].
==Reference==
==Reference==
Line 33: Line 37:
[[Category: Le-module]]
[[Category: Le-module]]
[[Category: Nidogen binding]]
[[Category: Nidogen binding]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:05:35 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:12:29 2008''

Revision as of 07:12, 28 July 2008

Image:1tle.png

Template:STRUCTURE 1tle

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

Template:ABSTRACT PUBMED 8648631

About this Structure

1TLE is a Single protein structure of sequence from Mus musculus. Full experimental information is available from OCA.

Reference

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

Page seeded by OCA on Mon Jul 28 10:12:29 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1tle"
Personal tools