Literature DB >> 1701030

Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains.

J H Wang1, Y W Yan, T P Garrett, J H Liu, D W Rodgers, R L Garlick, G E Tarr, Y Husain, E L Reinherz, S C Harrison.   

Abstract

The structure of an N-terminal fragment of CD4 has been determined to 2.4 A resolution. It has two tightly abutting domains connected by a continuous beta strand. Both have the immunoglobulin fold, but domain 2 has a truncated beta barrel and a non-standard disulphide bond. The binding sites for monoclonal antibodies, class II major histocompatibility complex molecules, and human immunodeficiency virus gp120 can be mapped on the molecular surface.

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Year:  1990        PMID: 1701030     DOI: 10.1038/348411a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  146 in total

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8.  Mutagenic stabilization and/or disruption of a CD4-bound state reveals distinct conformations of the human immunodeficiency virus type 1 gp120 envelope glycoprotein.

Authors:  Shi-Hua Xiang; Peter D Kwong; Rishi Gupta; Carlo D Rizzuto; David J Casper; Richard Wyatt; Liping Wang; Wayne A Hendrickson; Michael L Doyle; Joseph Sodroski
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9.  Functional epitope analysis of the human CD4 molecule: antibodies that inhibit human immunodeficiency virus type 1 gene expression bind to the immunoglobulin CDR3-like region of CD4.

Authors:  M Benkirane; M Hirn; D Carrière; C Devaux
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10.  The cytoplasmic tail of CD4 is required for inhibition of human immunodeficiency virus type 1 replication by antibodies that bind to the immunoglobulin CDR3-like region in domain 1 of CD4.

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