PDBsum entry 1mim

Immunoglobulin

PDB id: 1mim

Contents

Protein chains

210 a.a. *

215 a.a. *

Waters ×69

* Residue conservation analysis

PDB id:

1mim

Name:

Immunoglobulin

Title:

Igg fab fragment (cd25-binding)

Structure:

Chimeric sdz chi621. Chain: l. Fragment: igg fab. Engineered: yes. Other_details: murine anti-cd25 monoclonal antibody, rft5, chimerized with the constant regions of human 1gg1 heavy and kappa light chains. Chimeric sdz chi621. Chain: h. Fragment: igg fab.

Source:

Fragment: constant regions of 1gg1 heavy and kappa light chains. Homo sapiens. Human. Organism_taxid: 9606. Organism_taxid: 9606

Biol. unit:

Dimer (from PQS)

Resolution:

2.60Å R-factor: 0.196

Authors:

V.Mikol

Key ref:

V.Mikol (1996). Structure of the fab fragment of SDZ CHI621: a chimeric antibody against CD25. Acta Crystallogr D Biol Crystallogr, 52, 534-542. PubMed id: 15299676 DOI: 10.1107/S0907444996000704

Date:

04-Dec-95 Release date: 15-May-97

Protein chain

P01834  (IGKC_HUMAN) -  Immunoglobulin kappa constant from Homo sapiens

Seq: 107 a.a.

Struc: 210 a.a.

Protein chain

No UniProt id for this chain

Struc: 215 a.a.

DOI no: 10.1107/S0907444996000704

Acta Crystallogr D Biol Crystallogr 52:534-542 (1996)

PubMed id: 15299676

Structure of the fab fragment of SDZ CHI621: a chimeric antibody against CD25.

V.Mikol.

ABSTRACT

A specific drug targeted to the IL-2 receptor on activated T lymphocytes could limit acute immunological rejection during organ transplantation. A high-affinity monoclonal antibody directed against the alpha-chain of the IL-2 receptor (CD25) was chimerized with the constant regions of the human IgG1 heavy and k light chain resulting in SDZ CHII621 [Amlot, Rawlings, Fernando, Griffin, Heinrich, Schreier, Castaigne, Moore & Sweny (1995). Transplantation, 60, 748-756]. The Fab fragment of SDZ CHI621 has been purified and crystallized (P2(l), a = 39.58, b = 59.76, c = 102.09 A, beta = 99.98 degrees ). Its structure has been determined by molecular replacement and refined at 2.6 A to a crystallographic R factor of 19.7%. The protein exhibits the typical immunoglobulin fold. The complementary determining regions (CDR's) 1 and 2 of both heavy and light chains show similar conformations to other known reported structures whereas the CDR3 from the light chain seems to adopt a novel type of conformation. There is a network of interactions which maintain the CDR3 of both chains together and limit their solvent accessibility. The interaction between V(L) and C(L) has been strengthened by the chimerization whereas that between V(H) and C(H)1 has been weakened.

Selected figure(s)

Figure 4.
Fig. 4. Comparison of the Fab fragment of SDZ CHI621 with that of HyHel­5. Stereoviews of the superposition of the C '~ atoms trace of SDZ CHI621 (plain lnes) on that of HyHel5 (dotted lines) (Sheriff et al., 1987). Every 40th C '~ of SDZ CHI621 is labelld. The pictures representig mole­ cules were prepared with the program MOLSCRIPT (Kraulis, 1991).

Figure 5.
Fig. 5. Intermolecular interactions between the L3 and H3 loops of SDZ CHI621. The L3 and H3 loop residues and their labels are shown with black plain lines. Hydrogen bonds are represented as dashed lines and the values of the corresponding distances are given in Table 6.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1996, 52, 534-542) copyright 1996.

Figures were selected by an automated process.