CRYSTALLOGRAPHIC STUDIES AND PRIMARY STRUCTURE OF THE ANTITUMOR MONOCLONAL CC49 FAB'

被引：4

作者：

ABERGEL, C ^{[1
]}

PADLAN, EA ^{[1
]}

KASHMIRI, SVS ^{[1
]}

MILENIC, D ^{[1
]}

CALVO, B ^{[1
]}

SCHLOM, J ^{[1
]}

机构：

[1] NCI,TUMOR IMMUNOL & BIOL LAB,BETHESDA,MD 20892

来源：

PROTEINS-STRUCTURE FUNCTION AND GENETICS | 1993年 / 17卷 / 04期

关键词：

CRYSTALLIZATION; ANTITUMOR; ANTIBODY; PRIMARY STRUCTURE;

D O I：

10.1002/prot.340170411

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The Fab' of CC49, a murine monoclonal antibody directed against the human tumor-associated antigen TAG-72 has been crystallized. The crystals are monoclinic, space group P2(1) with cell parameters a = 115.6 angstrom, b = 116.4 angstrom, and c = 70.3 angstrom; beta = 97.8-degrees. The size of the unit cell is compatible with four Fab' molecules in the asymmetric unit. The Fab molecules are related by two approximately perpendicular pseudo-2-fold axes. One pseudo-2-fold axis is parallel to the crystallographic 2-fold axis and was found by inspection of the Harker section of the native Patterson map; the other was found by a self rotation function. The primary structures of the variable regions of the CC49 antibody light and heavy chains have been determined and are compared with those of the related antitumor antibody B72.3. (C) 1993 Wiley-Liss, Inc.*

引用

页码：438 / 443

页数：6

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