3i00

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[[Image:3i00.png|left|200px]]
 
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{{STRUCTURE_3i00| PDB=3i00 | SCENE= }}
{{STRUCTURE_3i00| PDB=3i00 | SCENE= }}
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===Crystal Structure of the huntingtin interacting protein 1 coiled coil domain===
===Crystal Structure of the huntingtin interacting protein 1 coiled coil domain===
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{{ABSTRACT_PUBMED_20179344}}
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==Disease==
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[[http://www.uniprot.org/uniprot/HIP1_HUMAN HIP1_HUMAN]] Note=A chromosomal aberration involving HIP1 is found in a form of chronic myelomonocytic leukemia (CMML). Translocation t(5;7)(q33;q11.2) with PDGFRB. The chimeric HIP1-PDGFRB transcript results from an in-frame fusion of the two genes. The reciprocal PDGFRB-HIP1 transcript is not expressed.
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==Function==
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[[http://www.uniprot.org/uniprot/HIP1_HUMAN HIP1_HUMAN]] Plays a role in clathrin-mediated endocytosis and trafficking. Involved in regulating AMPA receptor trafficking in the central nervous system in an NMDA-dependent manner. Enhances androgen receptor (AR)-mediated transcription. May act as a proapoptotic protein that induces cell death by acting through the intrinsic apoptosis pathway. Binds 3-phosphoinositides (via ENTH domain). May act through the ENTH domain to promote cell survival by stabilizing receptor tyrosine kinases following ligand-induced endocytosis. May play a functional role in the cell filament networks. May be required for differentiation, proliferation, and/or survival of somatic and germline progenitors.<ref>PMID:9147654</ref><ref>PMID:11007801</ref><ref>PMID:11532990</ref><ref>PMID:11577110</ref><ref>PMID:11889126</ref><ref>PMID:12163454</ref><ref>PMID:14732715</ref><ref>PMID:16027218</ref>
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(as it appears on PubMed at http://www.pubmed.gov), where 20179344 is the PubMed ID number.
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{{ABSTRACT_PUBMED_20179344}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:020179344</ref><references group="xtra"/>
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<ref group="xtra">PMID:020179344</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Brodsky, F M.]]
[[Category: Brodsky, F M.]]

Revision as of 08:59, 24 March 2013

Template:STRUCTURE 3i00

Contents

Crystal Structure of the huntingtin interacting protein 1 coiled coil domain

Template:ABSTRACT PUBMED 20179344

Disease

[HIP1_HUMAN] Note=A chromosomal aberration involving HIP1 is found in a form of chronic myelomonocytic leukemia (CMML). Translocation t(5;7)(q33;q11.2) with PDGFRB. The chimeric HIP1-PDGFRB transcript results from an in-frame fusion of the two genes. The reciprocal PDGFRB-HIP1 transcript is not expressed.

Function

[HIP1_HUMAN] Plays a role in clathrin-mediated endocytosis and trafficking. Involved in regulating AMPA receptor trafficking in the central nervous system in an NMDA-dependent manner. Enhances androgen receptor (AR)-mediated transcription. May act as a proapoptotic protein that induces cell death by acting through the intrinsic apoptosis pathway. Binds 3-phosphoinositides (via ENTH domain). May act through the ENTH domain to promote cell survival by stabilizing receptor tyrosine kinases following ligand-induced endocytosis. May play a functional role in the cell filament networks. May be required for differentiation, proliferation, and/or survival of somatic and germline progenitors.[1][2][3][4][5][6][7][8]

About this Structure

3i00 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Wilbur JD, Hwang PK, Brodsky FM, Fletterick RJ. Accommodation of structural rearrangements in the huntingtin-interacting protein 1 coiled-coil domain. Acta Crystallogr D Biol Crystallogr. 2010 Mar;66(Pt 3):314-8. Epub 2010 Feb 12. PMID:20179344 doi:10.1107/S0907444909054535
  1. ↑ Wanker EE, Rovira C, Scherzinger E, Hasenbank R, Walter S, Tait D, Colicelli J, Lehrach H. HIP-I: a huntingtin interacting protein isolated by the yeast two-hybrid system. Hum Mol Genet. 1997 Mar;6(3):487-95. PMID:9147654
  2. ↑ Hackam AS, Yassa AS, Singaraja R, Metzler M, Gutekunst CA, Gan L, Warby S, Wellington CL, Vaillancourt J, Chen N, Gervais FG, Raymond L, Nicholson DW, Hayden MR. Huntingtin interacting protein 1 induces apoptosis via a novel caspase-dependent death effector domain. J Biol Chem. 2000 Dec 29;275(52):41299-308. PMID:11007801 doi:10.1074/jbc.M008408200
  3. ↑ Waelter S, Scherzinger E, Hasenbank R, Nordhoff E, Lurz R, Goehler H, Gauss C, Sathasivam K, Bates GP, Lehrach H, Wanker EE. The huntingtin interacting protein HIP1 is a clathrin and alpha-adaptin-binding protein involved in receptor-mediated endocytosis. Hum Mol Genet. 2001 Aug 15;10(17):1807-17. PMID:11532990
  4. ↑ Mishra SK, Agostinelli NR, Brett TJ, Mizukami I, Ross TS, Traub LM. Clathrin- and AP-2-binding sites in HIP1 uncover a general assembly role for endocytic accessory proteins. J Biol Chem. 2001 Dec 7;276(49):46230-6. Epub 2001 Sep 27. PMID:11577110 doi:10.1074/jbc.M108177200
  5. ↑ Legendre-Guillemin V, Metzler M, Charbonneau M, Gan L, Chopra V, Philie J, Hayden MR, McPherson PS. HIP1 and HIP12 display differential binding to F-actin, AP2, and clathrin. Identification of a novel interaction with clathrin light chain. J Biol Chem. 2002 May 31;277(22):19897-904. Epub 2002 Mar 11. PMID:11889126 doi:10.1074/jbc.M112310200
  6. ↑ Rao DS, Hyun TS, Kumar PD, Mizukami IF, Rubin MA, Lucas PC, Sanda MG, Ross TS. Huntingtin-interacting protein 1 is overexpressed in prostate and colon cancer and is critical for cellular survival. J Clin Invest. 2002 Aug;110(3):351-60. PMID:12163454 doi:10.1172/JCI15529
  7. ↑ Hyun TS, Rao DS, Saint-Dic D, Michael LE, Kumar PD, Bradley SV, Mizukami IF, Oravecz-Wilson KI, Ross TS. HIP1 and HIP1r stabilize receptor tyrosine kinases and bind 3-phosphoinositides via epsin N-terminal homology domains. J Biol Chem. 2004 Apr 2;279(14):14294-306. Epub 2004 Jan 19. PMID:14732715 doi:10.1074/jbc.M312645200
  8. ↑ Mills IG, Gaughan L, Robson C, Ross T, McCracken S, Kelly J, Neal DE. Huntingtin interacting protein 1 modulates the transcriptional activity of nuclear hormone receptors. J Cell Biol. 2005 Jul 18;170(2):191-200. PMID:16027218 doi:10.1083/jcb.200503106

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