2c0l

From Proteopedia

Revision as of 15:17, 15 February 2008

TPR DOMAIN OF HUMAN PEX5P IN COMPLEX WITH HUMAN MSCP2

Overview

Peroxisomes require the translocation of folded and functional target, proteins of various sizes across the peroxisomal membrane. We have, investigated the structure and function of the principal import receptor, Pex5p, which recognizes targets bearing a C-terminal peroxisomal targeting, signal type 1. Crystal structures of the receptor in the presence and, absence of a peroxisomal target, sterol carrier protein 2, reveal major, structural changes from an open, snail-like conformation into a closed, circular conformation. These changes are caused by a long loop C terminal, to the 7-fold tetratricopeptide repeat segments. Mutations in residues of, this loop lead to defects in peroxisomal import in human fibroblasts. The, structure of the receptor/cargo complex demonstrates that the primary, receptor-binding site of the cargo is structurally and topologically, autonomous, enabling the cargo to retain its native structure and, function.

Disease

Known diseases associated with this structure: Adrenoleukodystrophy, neonatal OMIM:[600414], Zellweger syndrome OMIM:[600414]

About this Structure

2C0L is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Recognition of a functional peroxisome type 1 target by the dynamic import receptor pex5p., Stanley WA, Filipp FV, Kursula P, Schuller N, Erdmann R, Schliebs W, Sattler M, Wilmanns M, Mol Cell. 2006 Dec 8;24(5):653-63. PMID:17157249

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