View source for 5aea


==Crystal structure of human NCAM domain 1==
<StructureSection load='5aea' size='340' side='right'caption='[[5aea]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5aea]] is a 2 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=5AEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AEA 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</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=5aea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aea OCA], [https://pdbe.org/5aea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aea RCSB], [https://www.ebi.ac.uk/pdbsum/5aea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aea ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NCAM1_HUMAN NCAM1_HUMAN] This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CXCR4 is a G protein-coupled receptor with excellent potential as a therapeutic target for a range of clinical conditions including stem cell mobilization, cancer prognosis and treatment, fibrosis therapy and HIV. We report here the development of a fully human single-domain antibody-like scaffold termed an i-body, the engineering of which produces an i-body library possessing a long complementarity determining region (CDR) binding loop, and the isolation and characterisation of a panel of i-bodies with activity against human CXCR4. The CXCR4-specific i-bodies show antagonistic activity in a range of in vitro and in vivo assays including inhibition of HIV infection, cell migration and leukocyte recruitment but, importantly, not mobilization of hematopoietic stem cells. Epitope mapping of three CXCR4 i-bodies AM3-114, AM4-272 and AM3-523 revealed binding deep in the binding pocket of the receptor.

I-bodies: human single domain antibodies that antagonize chemokine receptor CXCR4.,Griffiths K, Dolezal O, Cao B, Nilsson SK, See HB, Pfleger KD, Roche M, Gorry PR, Pow A, Viduka K, Lim K, Lu BG, Chang DH, Murray-Rust TA, Kvansakul M, Perugini MA, Dogovski C, Doerflinger M, Zhang Y, Parisi K, Casey JL, Nuttall SD, Foley M J Biol Chem. 2016 Apr 1. pii: jbc.M116.721050. PMID:27036939<ref>PMID:27036939</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5aea" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Foley M]]
[[Category: Griffiths K]]
[[Category: Kvansakul M]]