[English] 日本語
![](img/lk-miru.gif)
- PDB-1klo: CRYSTAL STRUCTURE OF THREE CONSECUTIVE LAMININ-TYPE EPIDERMAL GRO... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1klo | ||||||
---|---|---|---|---|---|---|---|
Title | CRYSTAL STRUCTURE OF THREE CONSECUTIVE LAMININ-TYPE EPIDERMAL GROWTH FACTOR-LIKE (LE) MODULES OF LAMININ GAMMA1 CHAIN HARBORING THE NIDOGEN BINDING SITE | ||||||
![]() | LAMININ | ||||||
![]() | GLYCOPROTEIN | ||||||
Function / homology | ![]() laminin-1 complex / 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 / tissue development / hair cell differentiation ...laminin-1 complex / 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 / tissue development / hair cell differentiation / protein complex involved in cell-matrix adhesion / extracellular matrix structural constituent / hair follicle morphogenesis / positive regulation of muscle cell differentiation / positive regulation of cell adhesion / basement membrane / extracellular matrix disassembly / synaptic cleft / substrate adhesion-dependent cell spreading / animal organ morphogenesis / axon guidance / neuromuscular junction / neuron projection development / cell migration / chromatin organization / gene expression / protein-containing complex assembly / collagen-containing extracellular matrix / cell adhesion / extracellular region Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Stetefeld, J. / Mayer, U. / Timpl, R. / Huber, R. | ||||||
![]() | ![]() Title: Crystal structure of three consecutive laminin-type epidermal growth factor-like (LE) modules of laminin gamma1 chain harboring the nidogen binding site. Authors: Stetefeld, J. / Mayer, U. / Timpl, R. / Huber, R. #1: ![]() 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: ![]() 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 |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 54 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 39.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 362.9 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 364.6 KB | Display | |
Data in XML | ![]() | 4.8 KB | Display | |
Data in CIF | ![]() | 7.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 17141.363 Da / Num. of mol.: 1 Fragment: GAMMA-1 CHAIN, THREE CONSECUTIVE LAMININ-TYPE EPIDERMAL GROWTH FACTOR-LIKE (LE) MODULES Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
---|---|
#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 4.33 Å3/Da / Density % sol: 71.59 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal | *PLUS Density % sol: 4.1 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 22 ℃ / pH: 7 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Radiation | Scattering type: x-ray |
---|---|
Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.1 Å / Num. obs: 17012 / % possible obs: 91.4 % / Num. measured all: 29004 / Rmerge(I) obs: 0.07 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2.1→6 Å / σ(F): 0 /
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→6 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|