1MB8	Structural Protein	date	Aug 02, 2002
title	Crystal Structure Of The Actin Binding Domain Of Plectin
authors	B.Garcia-Alvarez, A.Bobkov, A.Sonnenberg, J.M.De Pereda
compound		source
Molecule: Plectin Chain: A Fragment: Residues 59-293 Synonym: Hd1 Engineered: Yes		Organism_scientific: Homo Sapiens Organism_common: Human Expression_system: Escherichia Coli Expression_system_common: Bacteria Expression_system_strain: Bl21(De3) Expression_system_vector_type: Plasmid Expression_system_plasmid: Pet15b
symmetry	Space Group: P 21 21 21	R_factor	0.212
crystal cell	length a length b length c angle alpha angle beta angle gamma 33.597 79.283 82.370 90.00 90.00 90.00
method	X-Ray Diffraction	resolution	2.15 Å
domain	The n-terminus interacts with actin, the c-terminus with vimentin, desmin, gfap, cytokeratins, lamin b; whereas both the n- and the c-terminus can bind integrin beta-4.
similarity	Contains 1 actin-binding domain. Contains 33 plectin repeats. Contains 2 calponin-homology (ch) domains. Belongs to the plakin or cytolinker family. Contains 4 spectrin repeats.[S10_plectin]
subunit	Homodimer or homotetramer.
post-translat. modifications	Phosphorylated by cdc2; regulates dissociation from intermediate filaments during mitosis (by similarity).
tissue	Widely expressed with highest levels in muscle, heart, placenta and spinal cord.
gene	PLEC1 (H. sapiens)
function	Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. May be involved not only in the crosslinking and stabilization of cytoskeletal intermediate filaments network, but also in the regulation of their dynamics. Could also bind muscle proteins such as actin to membrane complexes in muscle.
Gene Ontology	chain A: GO:0003779, GO:0005198, GO:0005200, GO:0005856, GO:0005882, GO:0005886, GO:0007016, GO:0008307
disease	Epidermolysis bullosa simplex,Ogna type Muscular dystrophy with epidermolysis bullosa simplex Defects in plec1 are the cause of epidermolysis bullosa simplex 1 (ebs1) [mim. 131950]; also called epidermolysis bullosa simplex ogna type. Ebs1 is an autosomal dominant form of epidermolysis bullosa simplex differentiated from the more generalized form of koebner [mim. 131900] and the localized form of weber and cockayne [mim. 131800] by the occurrence of skin bruising. Defects in plec1 are the cause of epidermolysis bullosa simplex with muscular dystrophy (md-ebs) [mim. 226670]. Md-ebs is an autosomal recessive disorder characterized by epidermal blister formation at the level of the hemidesmosome and associated with late-onset muscular dystrophy.
Primary reference	Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and integrin beta4., Garcia-Alvarez B, Bobkov A, Sonnenberg A, de Pereda JM, Structure (Camb) 2003 Jun;11(6):615-25. PMID:12791251

Data retrieval

Asymmetric unit, PDB entry: [header only] [complete with coordinates] (54 Kb) [Save to disk] Biological Unit Coordinates (1mb8.pdb1.gz) 44 Kb CSU: Contacts of Structural Units for 1MB8 Likely Quarternary Molecular Structure file(s) for 1MB8 Structure Factors (r1mb8sf.ent.Z) 92 Kb Retrieve 1MB8 in mmCIF format [Save to disk]

View 1MB8 in 3D

On Jmol, a nice Rasmol like molecule viewer. This is good for easiest viewing of basic structure. On AstexViewer, from MSD-EBI (viewer documentation). On RasMol (Install RasMol freeware) Here's help on how to use RasMol.

Visual 3D analysis of 1MB8

STING, shows the sequence and maps the locations of sequence residues or residue ranges onto the 3D structure. Noncovalent Bond Finder displays the closest contacts to ligand or interface, reports distances, walks over water bridges. GRASS (Graphical Representation and Analysis of Structure Server) Cartoon representation from PDB Cartoon Ramachandran plot from PDBSum

Structure-derived information

Electro Density related parameters from EDS Electron Density Server, at Upsala Dipole moment, from Dipole Server at Weizmann Institute Crystal Contacts, from CryCo at Weizmann Institute Classification of representative domains in scop (Structural Classification of Proteins)     - Domain d1mb8a2, region A:181-293 [Jmol] [rasmolscript] [script source]     - Domain d1mb8a1, region A:56-180 [Jmol] [rasmolscript] [script source] Fold representative 1mb8 from FSSP and Dali (Families of Structurally Similar Proteins)

Sequence-derived information

View one-letter amino acid or nucleotide sequence for each chain: [1mb8_A] SWISS-PROT database: [Q15148] [Q15149] [Q16640] Domain organization of [PLE1_HUMAN] by SWISSPFAM Conserved protein region description, domain view and alignment from family S10_plectin (PF03501) of Pfam. Alignments of the sequence of 1MB8 with the sequences similar proteins can be viewed for classification [PLE1_HUMAN] at ProtoMap. Click on "Neighbors List", then on the "See Alignments" button below the list. A sequence distance tree ("phylogenetic tree") can be viewed for 1ACL's classification [PLE1_HUMAN] at ProtoMap. Click on the Cluster number.

Other resources with information on 1MB8

InterPro: IPR002017 , IPR001589 , IPR005326 , IPR001715 , IPR001101 MMDB (Entrez's Structure Database)

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