2re9

From Proteopedia

Revision as of 10:35, 23 January 2008

Crystal structure of TL1A at 2.1 A

Overview

The TNF family has been one of the most intensively studied protein, families in the past two decades and it has rapidly expanded through the, era of genomics and bioinformatics. However, the structural basis of the, functional and interactional similarities and differences of this family, is poorly understood. TL1A is a recently identified TNF family member that, has received increasing attention. Here, the crystal structure of human, TL1A is reported. TL1A forms a homotrimer with each monomer assuming a, jellyroll beta-sandwich fold. The CD loop in TL1A is the longest among the, TNF ligand members with known structure and the AA' loop in TL1A is the, second longest after that in TRAIL, where part of it is disordered. Both, these loops are known to participate in receptor binding in, TNFbeta/LTalpha. The AA' loop may be very different in other TL1A variants, if the overall fold is to be preserved.

About this Structure

2RE9 is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

X-ray crystal structure of TNF ligand family member TL1A at 2.1A., Jin T, Guo F, Kim S, Howard A, Zhang YZ, Biochem Biophys Res Commun. 2007 Dec 7;364(1):1-6. Epub 2007 Oct 1. PMID:17935696

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