PDBsum entry 1tle

Glycoprotein

PDB id: 1tle

Contents

Protein chain

58 a.a. *

* Residue conservation analysis

PDB id:

1tle

Name:

Glycoprotein

Title:

Le (laminin-type egf-like) module giii4 in solution at ph 3.5 and 290 k, nmr, 14 structures

Structure:

Laminin. Chain: a. Fragment: nidogen binding le module of the laminin gamma1 chain, module giii4. Synonym: laminin-type egf-like. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Tissue: basement membrane. Gene: lamc1. Expressed in: mus musculus. Expression_system_taxid: 10090.

NMR struc:

14 models

Authors:

R.Baumgartner,M.Czisch,U.Mayer,E.P.Schl,R.Huber,R.Timpl,T.A.Holak

Key ref:

R.Baumgartner et al. (1996). Structure of the nidogen binding LE module of the laminin gamma1 chain in solution. J Mol Biol, 257, 658-668. PubMed id: 8648631 DOI: 10.1006/jmbi.1996.0192

Date:

26-Jan-96 Release date: 12-Feb-97

Protein chain

P02468  (LAMC1_MOUSE) -  Laminin subunit gamma-1 from Mus musculus

Seq: 1607 a.a.

Struc: 58 a.a.

DOI no: 10.1006/jmbi.1996.0192

J Mol Biol 257:658-668 (1996)

PubMed id: 8648631

Structure of the nidogen binding LE module of the laminin gamma1 chain in solution.

R.Baumgartner, M.Czisch, U.Mayer, E.Pöschl, R.Huber, R.Timpl, T.A.Holak.

ABSTRACT

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.

Selected figure(s)

Figure 9.
Figure 9. Best superposition of g1III4 module on the structure of mouse EGF. g1III4 is shown in green and EGF in red (Kohda & Ihagaki, 1992).

Figure 10.
Figure 10. Best superposition of the constrained energy minimized average structure (SA)m for g1III4 with the X-ray structure (Stetefeld et al., 1996).

The above figures are reprinted by permission from Elsevier: J Mol Biol (1996, 257, 658-668) copyright 1996.

Figures were selected by an automated process.