PDBsum entry 4igi

Cell adhesion

PDB id

4igi

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Contents

			Protein chain

					197 a.a.

			Waters ×240

PDB id:

4igi

Links

Name:

Cell adhesion

Title:

Crystal structure of the collagen vi alpha3 n5 domain

Structure:

Collagen alpha3(vi). Chain: a. Fragment: collagen vi alpha3 n5, unp residues 1022-1224. Engineered: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Strain: c57bl6. Gene: col6a3. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.20Å

R-factor:

0.121

R-free:

0.148

Authors:

H.Mikolajek,A.K.A.Becker,M.Paulsson,R.Wagener,J.M.Werner

Key ref:

A.K.Becker et al. (2014). A structure of a collagen VI VWA domain displays N and C termini at opposite sides of the protein. Structure, 22, 199-208. PubMed id: 24332716

Date:

17-Dec-12

Release date:

18-Dec-13

PROCHECK

	Headers

	References

Protein chain

E9PWQ3 (E9PWQ3_MOUSE) - von Willebrand factor A domain-containing protein 1 from Mus musculus

Seq: Struc:

Seq: Struc:

Seq: Struc:

Seq: Struc:

Seq: Struc:

Seq: Struc:

Seq: Struc:					3284 a.a. 197 a.a.

Key:

PfamA domain

Secondary structure

CATH domain

	Structure 22:199-208 (2014)
PubMed id: 24332716

A structure of a collagen VI VWA domain displays N and C termini at opposite sides of the protein.
A.K.Becker, H.Mikolajek, M.Paulsson, R.Wagener, J.M.Werner.

ABSTRACT

Von Willebrand factor A (VWA) domains are versatile protein interaction domains with N and C termini in close proximity placing spatial constraints on overall protein structure. The 1.2 Å crystal structures of a collagen VI VWA domain and a disease-causing point mutant show C-terminal extensions that place the N and C termini at opposite ends. This allows a "beads-on-a-string" arrangement of multiple VWA domains as observed for ten N-terminal domains of the collagen VI α3 chain. The extension is linked to the core domain by a salt bridge and two hydrophobic patches. Comparison of the wild-type and a muscular dystrophy-associated mutant structure identifies a potential perturbation of a protein interaction interface and indeed, the secretion of mutant collagen VI tetramers is affected. Homology modeling is used to locate a number of disease-associated mutations and analyze their structural impact, which will allow mechanistic analysis of collagen-VI-associated muscular dystrophy phenotypes.