PDBsum entry: 2ka3

Structural protein

PDB id: 2ka3

Contents

Protein chains

131 a.a. *

* Residue conservation analysis

PDB id:

2ka3

Name:

Structural protein

Title:

Structure of emilin-1 c1q-like domain

Structure:

Emilin-1. Chain: a, b, c. Fragment: c-terminal domain, c1q domain, unp residues 867- 1016. Synonym: elastin microfibril interface-located protein 1, elastin microfibril interfacer 1. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: em1, emilin1. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_variant: m15 cells.

NMR struc:

10 models

Authors:

G.Verdone,A.Corazza,S.A.Colebrooke,D.O.Cicero,T.Eliseo, J.Boyd,R.Doliana,F.Fogolari,P.Viglino,A.Colombatti, I.D.Campbell,G.Esposito

Key ref:

G.Verdone et al. (2009). NMR-based homology model for the solution structure of the C-terminal globular domain of EMILIN1. J Biomol Nmr, 43, 79-96. PubMed id: 19023665 DOI: 10.1007/s10858-008-9290-y

Date:

30-Oct-08 Release date: 25-Nov-08

Protein chains

Q9Y6C2  (EMIL1_HUMAN) -  EMILIN-1

Seq: 1016 a.a.

Struc: 131 a.a.

DOI no: 10.1007/s10858-008-9290-y

J Biomol Nmr 43:79-96 (2009)

PubMed id: 19023665

NMR-based homology model for the solution structure of the C-terminal globular domain of EMILIN1.

G.Verdone, A.Corazza, S.A.Colebrooke, D.Cicero, T.Eliseo, J.Boyd, R.Doliana, F.Fogolari, P.Viglino, A.Colombatti, I.D.Campbell, G.Esposito.

ABSTRACT

EMILIN1 is a glycoprotein of elastic tissues that has been recently linked to the pathogenesis of hypertension. The protein is formed by different independently folded structural domains whose role has been partially elucidated. In this paper the solution structure, inferred from NMR-based homology modelling of the C-terminal trimeric globular C1q domain (gC1q) of EMILIN1, is reported. The high molecular weight and the homotrimeric structure of the protein required the combined use of highly deuterated (15)N, (13)C-labelled samples and TROSY experiments. Starting from a homology model, the protein structure was refined using heteronuclear residual dipolar couplings, chemical shift patterns, NOEs and H-exchange data. Analysis of the gC1q domain structure of EMILIN1 shows that each protomer of the trimer adopts a nine-stranded beta sandwich folding topology which is related to the conformation observed for other proteins of the family. Distinguishing features, however, include a missing edge-strand and an unstructured 19-residue loop. Although the current data do not allow this loop to be precisely defined, the available evidence is consistent with a flexible segment that protrudes from each subunit of the globular trimeric assembly and plays a key role in inter-molecular interactions between the EMILIN1 gC1q homotrimer and its integrin receptor alpha4beta1.