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 2.20&Aring;" /> '''CRYSTAL STRUCTURE O...)
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'''CRYSTAL STRUCTURE OF THE PTS1 COMPLEXED TO THE TPR REGION OF HUMAN PEX5'''<br />
'''CRYSTAL STRUCTURE OF THE PTS1 COMPLEXED TO THE TPR REGION OF HUMAN PEX5'''<br />
==Overview==
==Overview==
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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.
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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==
==Disease==
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==About this Structure==
==About this Structure==
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1FCH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FCH OCA].
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1FCH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FCH OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Berg, J.M.]]
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[[Category: Berg, J M.]]
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[[Category: Geisbrecht, B.V.]]
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[[Category: Geisbrecht, B V.]]
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[[Category: Gould, S.J.]]
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[[Category: Gould, S J.]]
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[[Category: Jr., G.J.Gatto.]]
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[[Category: Jr., G J.Gatto.]]
[[Category: helical repeat]]
[[Category: helical repeat]]
[[Category: protein-peptide complex]]
[[Category: protein-peptide complex]]
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[[Category: tpr]]
[[Category: tpr]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:51:30 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:37:17 2008''

Revision as of 10:37, 21 February 2008


1fch, resolution 2.20Å

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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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