3n1f

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:06, 6 September 2023) (edit) (undo)
 
(4 intermediate revisions not shown.)
Line 1: Line 1:
-
{{STRUCTURE_3n1f| PDB=3n1f | SCENE= }}
 
-
===Crystal Structure of IhhN bound to CDOFn3===
 
-
{{ABSTRACT_PUBMED_20519495}}
 
-
==Disease==
+
==Crystal Structure of IhhN bound to CDOFn3==
-
[[http://www.uniprot.org/uniprot/CDON_HUMAN CDON_HUMAN]] Defects in CDON are the cause of holoprosencephaly type 11 (HPE11) [MIM:[http://omim.org/entry/614226 614226]]. HPE11 is a structural anomaly of the brain, in which the developing forebrain fails to correctly separate into right and left hemispheres. Holoprosencephaly is genetically heterogeneous and associated with several distinct facies and phenotypic variability.
+
<StructureSection load='3n1f' size='340' side='right'caption='[[3n1f]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3n1f]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N1F FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3n1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n1f OCA], [https://pdbe.org/3n1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n1f RCSB], [https://www.ebi.ac.uk/pdbsum/3n1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n1f ProSAT]</span></td></tr>
 +
</table>
 +
== Disease ==
 +
[https://www.uniprot.org/uniprot/IHH_HUMAN IHH_HUMAN] Brachydactyly type A1;Acrocapitofemoral dysplasia. Defects in IHH are the cause of brachydactyly type A1 (BDA1) [MIM:[https://omim.org/entry/112500 112500]. BDA1 is an autosomal dominant disorder characterized by middle phalanges of all the digits rudimentary or fused with the terminal phalanges. The proximal phalanges of the thumbs and big toes are short.<ref>PMID:11455389</ref> <ref>PMID:12384778</ref> Defects in IHH are a cause of acrocapitofemoral dysplasia (ACFD) [MIM:[https://omim.org/entry/607778 607778]. ACFD is a disorder characterized by short stature of variable severity with postnatal onset. The most constant radiographic abnormalities are observed in the tubular bones of the hands and in the proximal part of the femur. Cone-shaped epiphyses or a similar epiphyseal configuration with premature epimetaphyseal fusion result in shortening of the skeletal components involved. Cone-shaped epiphyses were also present to a variable extent at the shoulders, knees, and ankles.<ref>PMID:12632327</ref>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/IHH_HUMAN IHH_HUMAN] Intercellular signal essential for a variety of patterning events during development. Binds to the patched (PTC) receptor, which functions in association with smoothened (SMO), to activate the transcription of target genes. Implicated in endochondral ossification: may regulate the balance between growth and ossification of the developing bones. Induces the expression of parathyroid hormone-related protein (PTHRP) (By similarity).
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n1/3n1f_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3n1f ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Hedgehog (Hh) signaling proteins stimulate cell proliferation, differentiation, and tissue patterning at multiple points in animal development. A single Hh homolog is present in Drosophila, but three Hh homologs, Sonic Hh, Indian Hh, and Desert Hh, are present in mammals. Distribution, movement, and reception of Hh signals are tightly regulated, and abnormal Hh signaling is associated with developmental defects and cancer. In addition to the integral membrane proteins Patched and Smoothened, members of the Drosophila Ihog family of adhesion-like molecules have recently been shown to bind Hh proteins with micromolar affinity and positively regulate Hh signaling. Cell adhesion molecule-related, down-regulated by oncogenes (CDO) and Brother of CDO (BOC) are the closest mammalian relatives of Drosophila Ihog, and CDO binds Sonic Hh with micromolar affinity and positively regulates Hh signaling. Despite these similarities, structural and biochemical studies have shown that Ihog and CDO utilize nonorthologous domains and completely different binding modes to interact with cognate Hh proteins. We report here biochemical and x-ray structural studies of Sonic, Indian, and Desert Hh proteins both alone and complexed with active domains of CDO and BOC. These results show that all mammalian Hh proteins bind CDO and BOC in the same manner. We also show that interactions between Hh proteins and CDO are weakened at low pH. Formation of Hh-mediated Hh oligomers is thought to be an important feature of normal Hh signaling, but no conserved self-interaction between Hh proteins is apparent from inspection of 14 independent Hh-containing crystal lattices.
-
==Function==
+
All mammalian Hedgehog proteins interact with cell adhesion molecule, down-regulated by oncogenes (CDO) and brother of CDO (BOC) in a conserved manner.,Kavran JM, Ward MD, Oladosu OO, Mulepati S, Leahy DJ J Biol Chem. 2010 Aug 6;285(32):24584-90. Epub 2010 Jun 1. PMID:20519495<ref>PMID:20519495</ref>
-
[[http://www.uniprot.org/uniprot/CDON_HUMAN CDON_HUMAN]] Component of a cell-surface receptor complex that mediates cell-cell interactions between muscle precursor cells. Promotes differentiation of myogenic cells (By similarity).
+
-
==About this Structure==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[3n1f]] is a 4 chain structure with 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=3N1F OCA].
+
</div>
-
 
+
<div class="pdbe-citations 3n1f" style="background-color:#fffaf0;"></div>
-
==Reference==
+
== References ==
-
<ref group="xtra">PMID:020519495</ref><references group="xtra"/><references/>
+
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Kavran, J M.]]
+
[[Category: Large Structures]]
-
[[Category: Leahy, D J.]]
+
[[Category: Kavran JM]]
-
[[Category: Binding site]]
+
[[Category: Leahy DJ]]
-
[[Category: Cell adhesion molecule]]
+
-
[[Category: Cell cycle protein]]
+
-
[[Category: Cell line]]
+
-
[[Category: Cell surface]]
+
-
[[Category: Conserved sequence]]
+
-
[[Category: Fibronectin]]
+
-
[[Category: Hedgehog protein]]
+
-
[[Category: Immunoglobulin g]]
+
-
[[Category: Membrane glycoprotein]]
+
-
[[Category: Membrane protein]]
+
-
[[Category: Protein binding]]
+
-
[[Category: Receptor]]
+
-
[[Category: Sequence homology]]
+
-
[[Category: Signal transduction]]
+
-
[[Category: Tertiary]]
+
-
[[Category: Tumor suppressor protein]]
+

Current revision

Crystal Structure of IhhN bound to CDOFn3

PDB ID 3n1f

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3n1f"
Personal tools