1fch
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(New page: 200px<br /> <applet load="1fch" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fch, resolution 2.20Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 14:45, 12 November 2007
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CRYSTAL STRUCTURE OF THE PTS1 COMPLEXED TO THE TPR REGION OF HUMAN PEX5
Contents |
Overview
Many proteins contain targeting signals within their sequences that, specify their delivery to particular organelles. The peroxisomal targeting, signal-1 (PTS1) is a C-terminal tripeptide that is sufficient to direct, proteins into peroxisomes. The PTS1 sequence closely approximates, Ser-Lys-Leu-COO-. PEX5, the receptor for PTS1, interacts with the signal, via a series of tetratricopeptide repeats (TPRs) within its C-terminal, half. Here we report the crystal structure of a fragment of human PEX5, that includes all seven predicted TPR motifs in complex with a, pentapeptide containing a PTS1 sequence. Two clusters of three TPRs almost, completely surround the peptide, while a hinge region, previously, identified as TPR4, forms a distinct structure that enables the two sets, of TPRs to form a single binding site. This structure reveals the, molecular basis for PTS1 recognition and demonstrates a novel mode of, TPR-peptide interaction.
Disease
Known diseases associated with this structure: Adrenoleukodystrophy, neonatal OMIM:[600414], Zellweger syndrome OMIM:[600414]
About this Structure
1FCH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5., Gatto GJ Jr, Geisbrecht BV, Gould SJ, Berg JM, Nat Struct Biol. 2000 Dec;7(12):1091-5. PMID:11101887
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