PDBsum entry 3b5h

Cell invasion

PDB id: 3b5h

Contents

Protein chain

181 a.a. *

Ligands

ACT

Waters ×30

* Residue conservation analysis

PDB id:

3b5h

Name:

Cell invasion

Title:

Crystal structure of the extracellular portion of hab18g/cd147

Structure:

Cervical emmprin. Chain: a, b, c, d. Fragment: extracellular portion, unp residues 22-205. Synonym: hab18g/cd147. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: bsg. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.80Å R-factor: 0.245 R-free: 0.294

Authors:

X.-L.Yu,Z.-N.Chen

Key ref:

X.L.Yu et al. (2008). Crystal Structure of HAb18G/CD147: IMPLICATIONS FOR IMMUNOGLOBULIN SUPERFAMILY HOMOPHILIC ADHESION. J Biol Chem, 283, 18056-18065. PubMed id: 18430721 DOI: 10.1074/jbc.M802694200

Date:

26-Oct-07 Release date: 06-May-08

Protein chains

P35613  (BASI_HUMAN) -  Basigin from Homo sapiens

Seq: 385 a.a.

Struc: 181 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1074/jbc.M802694200

J Biol Chem 283:18056-18065 (2008)

PubMed id: 18430721

Crystal Structure of HAb18G/CD147: IMPLICATIONS FOR IMMUNOGLOBULIN SUPERFAMILY HOMOPHILIC ADHESION.

X.L.Yu, T.Hu, J.M.Du, J.P.Ding, X.M.Yang, J.Zhang, B.Yang, X.Shen, Z.Zhang, W.D.Zhong, N.Wen, H.Jiang, P.Zhu, Z.N.Chen.

ABSTRACT

CD147, a member of the immunoglobulin superfamily (IgSF), plays fundamental roles in intercellular interactions in numerous pathological and physiological processes. Importantly, our previous studies have demonstrated that HAb18G/CD147 is a novel hepatocellular carcinoma (HCC)-associated antigen, and HAb18G/CD147 stimulates adjacent fibroblasts and HCC cells to produce elevated levels of several matrix metalloproteinases, facilitating invasion and metastasis of HCC cells. In addition, HAb18G/CD147 has also been shown to be a novel universal cancer biomarker for diagnosis and prognostic assessment of a wide range of cancers. However, the structural basis underlying the multifunctional character of CD147 remains unresolved. We report here the crystal structure of the extracellular portion of HAb18G/CD147 at 2.8A resolution. The structure comprises an N-terminal IgC2 domain and a C-terminal IgI domain, which are connected by a 5-residue flexible linker. This unique C2-I domain organization is distinct from those of other IgSF members. Four homophilic dimers exist in the crystal and adopt C2-C2 and C2-I dimerization rather than V-V dimerization commonly found in other IgSF members. This type of homophilic association thus presents a novel model for homophilic interaction between C2 domains of IgSF members. Moreover, the crystal structure of HAb18G/CD147 provides a good structural explanation for the established multifunction of CD147 mediated by homo/hetero-oligomerizations and should represent a general architecture of other CD147 family members.

Selected figure(s)

Figure 3.
FIGURE 3. The sequence alignment among CD147, neuroplastin, and embigin from various species. Bars and helices symbolize secondary structures. The conserved residues mentioned in the text are shaded and numbered. The disulfide bonds and N-glycosylation sites are also denoted.

Figure 4.
FIGURE 4. Structural superposition of HAb18G/CD147 domain 2 with the heavy-chain variable domain of Fab New and domain 1. A, C[ ]superposition of HAb18G/CD147 domain 2 with the VH domain of Fab New. B, C[ ]superposition of HAb18G/CD147 domain 2 with domain 1. Molecules are depicted as ribbons with strands labeled according to convention. The parenthesized letters represent strands from Fab (A) or domain 2 (B). The C-C' β-bulge of domain 2 is similar to that of Fab VH domain but absent in domain 1.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2008, 283, 18056-18065) copyright 2008.

Figures were selected by an automated process.