8hlo
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8hlo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HLO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HLO FirstGlance]. <br> | <table><tr><td colspan='2'>[[8hlo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HLO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HLO FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.168Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=8hlo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hlo OCA], [https://pdbe.org/8hlo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hlo RCSB], [https://www.ebi.ac.uk/pdbsum/8hlo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hlo ProSAT]</span></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=8hlo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hlo OCA], [https://pdbe.org/8hlo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hlo RCSB], [https://www.ebi.ac.uk/pdbsum/8hlo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hlo ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ASAP1_MOUSE ASAP1_MOUSE] May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types. Plays a role in ciliogenesis (By similarity). Posseses phosphatidylinositol 4,5-bisphosphate-dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2. | [https://www.uniprot.org/uniprot/ASAP1_MOUSE ASAP1_MOUSE] May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types. Plays a role in ciliogenesis (By similarity). Posseses phosphatidylinositol 4,5-bisphosphate-dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | SH3 domains are common protein binding modules. The target sequence of SH3 domains is usually a proline-rich motif (PRM) containing a minimal "PxxP" sequence. The mechanism of how different SH3 domains specifically choose their targets from vast PxxP-containing sequences is still not very clear, as many reported SH3/PRM interactions are weak and promiscuous. Here, we identified the binding of the SH3 domain of ASAP1 to the PRM of MICAL1 with a sub-muM binding affinity, and determined the crystal structure of ASAP1-SH3 and MICAL1-PRM complex. Our structural and biochemical analyses revealed that the target-binding pocket of ASAP1-SH3 contains two negatively charged patches to recognize the "xPx + Px+" sequence in MICAL1-PRM and consequently strengthen the interaction, differing from the typical SH3/PRM interaction. This unique PRM-binding pocket is also found in the SH3 domains of GTPase Regulator associated with focal adhesion kinase (GRAF) and Src kinase associated phosphoprotein 1 (SKAP1), which we named SH3(AGS). In addition, we searched the Swiss-Prot database and found ~130 proteins with the SH3(AGS)-binding PRM in silico. Finally, gene ontology analysis suggests that the strong interaction between the SH3(AGS)-containing proteins and their targets may play roles in actin cytoskeleton regulation and vesicle trafficking. | ||
| + | |||
| + | Crystal Structure of the SH3 Domain of ASAP1 in Complex with the Proline Rich Motif (PRM) of MICAL1 Reveals a Unique SH3/PRM Interaction Mode.,Jia X, Lin L, Xu S, Li L, Wei Z, Yu C, Niu F Int J Mol Sci. 2023 Jan 11;24(2):1414. doi: 10.3390/ijms24021414. PMID:36674928<ref>PMID:36674928</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8hlo" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of ASAP1-SH3 and MICAL1-PRM complex
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Categories: Homo sapiens | Large Structures | Mus musculus | Niu F | Wei Z | Yu C
