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- PDB-1tle: LE (LAMININ-TYPE EGF-LIKE) MODULE GIII4 IN SOLUTION AT PH 3.5 AND... -

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Basic information

Entry
Database: PDB / ID: 1tle
TitleLE (LAMININ-TYPE EGF-LIKE) MODULE GIII4 IN SOLUTION AT PH 3.5 AND 290 K, NMR, 14 STRUCTURES
ComponentsLAMININ
KeywordsGLYCOPROTEIN / EXTRACELLULAR MATRIX PROTEIN / NIDOGEN BINDING / LE-MODULE
Function / homology
Function and homology information


laminin-10 complex / tissue morphogenesis / hair follicle cell proliferation / regulation of basement membrane organization / hemidesmosome assembly / glycosphingolipid binding / positive regulation of integrin-mediated signaling pathway / hair cell differentiation / protein complex involved in cell-matrix adhesion / extracellular matrix structural constituent ...laminin-10 complex / tissue morphogenesis / hair follicle cell proliferation / regulation of basement membrane organization / hemidesmosome assembly / glycosphingolipid binding / positive regulation of integrin-mediated signaling pathway / hair cell differentiation / protein complex involved in cell-matrix adhesion / extracellular matrix structural constituent / hair follicle morphogenesis / positive regulation of muscle cell differentiation / basement membrane / extracellular matrix disassembly / synaptic cleft / positive regulation of cell adhesion / neuromuscular junction / neuron projection development / cell migration / : / chromatin organization / protein-containing complex assembly / gene expression / cell adhesion / extracellular region
Similarity search - Function
Laminin IV / Laminin B (Domain IV) / Laminin IV type A domain profile. / Laminin B domain / Laminin, N-terminal / : / Laminin N-terminal (Domain VI) / Laminin N-terminal domain profile. / Laminin N-terminal domain (domain VI) / : ...Laminin IV / Laminin B (Domain IV) / Laminin IV type A domain profile. / Laminin B domain / Laminin, N-terminal / : / Laminin N-terminal (Domain VI) / Laminin N-terminal domain profile. / Laminin N-terminal domain (domain VI) / : / Laminin/attractin EGF domain / Laminin-type EGF-like (LE) domain profile. / Laminin-type EGF-like (LE) domain signature. / Laminin-type epidermal growth factor-like domai / Laminin EGF domain / Laminin-type EGF domain / Laminin / Laminin / Epidermal growth factor-like domain. / EGF-like domain signature 1. / EGF-like domain signature 2. / EGF-like domain / Ribbon / Mainly Beta
Similarity search - Domain/homology
Laminin subunit gamma-1
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodSOLUTION NMR
AuthorsBaumgartner, R. / Czisch, M. / Mayer, U. / Schl, E.P. / Huber, R. / Timpl, R. / Holak, T.A.
Citation
Journal: J.Mol.Biol. / Year: 1996
Title: Structure of the nidogen binding LE module of the laminin gamma1 chain in solution.
Authors: Baumgartner, R. / Czisch, M. / Mayer, U. / Poschl, E. / Huber, R. / Timpl, R. / Holak, T.A.
#1: Journal: Embo J. / Year: 1994
Title: Two Non-Contiguous Regions Contribute to Nidogen Binding to a Single Egf-Like Motif of the Laminin Gamma 1 Chain
Authors: Poschl, E. / Fox, J.W. / Block, D. / Mayer, U. / Timpl, R.
#2: Journal: Embo J. / Year: 1993
Title: A Single Egf-Like Motif of Laminin is Responsible for High Affinity Nidogen Binding
Authors: Mayer, U. / Nischt, R. / Poschl, E. / Mann, K. / Fukuda, K. / Gerl, M. / Yamada, Y. / Timpl, R.
History
DepositionJan 26, 1996Processing site: BNL
Revision 1.0Feb 12, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site
Revision 1.4Oct 30, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: LAMININ


Theoretical massNumber of molelcules
Total (without water)6,3521
Polymers6,3521
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)14 / -
Representative

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Components

#1: Protein LAMININ / LAMININ-TYPE EGF-LIKE


Mass: 6352.206 Da / Num. of mol.: 1
Fragment: NIDOGEN BINDING LE MODULE OF THE LAMININ GAMMA1 CHAIN, MODULE GIII4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Tissue: BASEMENT MEMBRANE / Gene: LAMC1 / Plasmid: PCEP4 / Gene (production host): LAMC1 / Production host: Mus musculus (house mouse) / References: UniProt: P02468
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Sample conditionspH: 3.5 / Temperature: 290 K
Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
NMR softwareName: X-PLOR / Version: 3.1 / Developer: BRUNGER / Classification: refinement
NMR ensembleConformers submitted total number: 14

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