CLONING AND SEQUENCING OF A TROPHOBLAST-ENDOTHELIAL-ACTIVATED LYMPHOCYTE SURFACE PROTEIN - CDNA SEQUENCE AND GENOMIC STRUCTURE

被引：10

作者：

VOLAND, JR ^{[1
]}

WYZYKOWSKI, RJ ^{[1
]}

HUANG, M ^{[1
]}

DUTTON, RW ^{[1
]}

机构：

[1] UNIV CALIF SAN DIEGO,CTR CANC,LA JOLLA,CA 92093

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1992年 / 89卷 / 21期

关键词：

LEUCINE ZIPPER; LYMPHOCYTE ACTIVATION ANTIGEN; MYC; NUCLEAR PROTOONCOGENES; SYNCYTIOTROPHOBLAST ANTIGEN;

D O I：

10.1073/pnas.89.21.10425

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

We have previously described the distribution of a surface glycoprotein recognized by monoclonal antibody B721. We now report the molecular characterization of this molecule at the protein, cDNA, and genomic level. A 75-kDa glycoprotein can be immunoprecipitated from B721+ tissues. We have isolated a near full-length cDNA containing the complete coding region and a full-length genomic clone. We present evidence that this protein has similarity to several classes of nuclear transcription factors, particularly the myc family of proteins. The 721P protein was found to have a leucine zipper-like structure, a possible basic region immediately upstream from the leucine zipper, and a protein kinase A phosphorylation site. 721P protein is encoded by a gene distinct from any deposited in existing data bases, and displays several features associated with proteins involved in signal transduction and gene regulation.

引用

页码：10425 / 10429

页数：5

共 28 条

[1] MAX - A HELIX-LOOP-HELIX ZIPPER PROTEIN THAT FORMS A SEQUENCE-SPECIFIC DNA-BINDING COMPLEX WITH MYC [J].