PDBsum entry 2i1p

Ligand binding protein

PDB id: 2i1p

Contents

Protein chain

48 a.a. *

Metals

_CA

* Residue conservation analysis

PDB id:

2i1p

Name:

Ligand binding protein

Title:

Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin

Structure:

Low-density lipoprotein receptor-related protein 2. Chain: a. Fragment: meg-a12. Synonym: megalin, glycoprotein 330, gp330. Engineered: yes

Source:

Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

C.A.Wolf,F.Dancea,M.Shi,V.Bade-Noskova,H.Rueterjans,D.Kerjaschki, C.Luecke

Key ref:

C.A.Wolf et al. (2007). Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin. J Biomol Nmr, 37, 321-328. PubMed id: 17245526

Date:

14-Aug-06 Release date: 13-Feb-07

Protein chain

P98158  (LRP2_RAT) -  Low-density lipoprotein receptor-related protein 2 from Rattus norvegicus

Seq: 4660 a.a.

Struc: 48 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

J Biomol Nmr 37:321-328 (2007)

PubMed id: 17245526

Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin.

C.A.Wolf, F.Dancea, M.Shi, V.Bade-Noskova, H.Rüterjans, D.Kerjaschki, C.Lücke.

ABSTRACT

Megalin, an approx. 600 kDa transmembrane glycoprotein that acts as multi-ligand transporter, is a member of the low density lipoprotein receptor gene family. Several cysteine-rich repeats, each consisting of about 40 residues, are responsible for the multispecific binding of ligands. The solution structure of the twelfth cysteine-rich ligand-binding repeat with class A motif found in megalin features two short beta-strands and two helical turns, yielding the typical fold with a I-III, II-V and IV-VI disulfide bridge connectivity pattern and a calcium coordination site at the C-terminal end. The resulting differences in electrostatic surface potential compared to other ligand-binding modules of this gene family, however, may be responsible for the functional divergence.