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1iak

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HISTOCOMPATIBILITY ANTIGEN I-AK

Structural highlights

1iak is a 3 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HA2K_MOUSE

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

We have determined the structure of murine MHC class II I-Ak in complex with a naturally processed peptide from hen egg lysozyme (HEL residues 50-62) at 1.9 A resolution. These results provide a structural basis for the I-Ak peptide-binding motif. Binding is established by the deep burial of five anchor side chains into specific pockets of the I-Ak binding groove, with a zen-like fit of an aspartic acid in the P1 pocket. We also show that in the I-Ak alpha chain, a bulge occurs in the first strand of the peptide-binding platform, an insertion probably common to all I-A and HLA-DQ alleles. The I-Ak beta chain has a deletion in the helical region adjacent to the P7 pocket and an insertion in the helical region neighboring the P1 pocket. As a result of these structural features, the extended HEL peptide dips low into the center of the I-Ak groove and reaches toward solvent at its C-terminal end.

Crystal structure of I-Ak in complex with a dominant epitope of lysozyme.,Fremont DH, Monnaie D, Nelson CA, Hendrickson WA, Unanue ER Immunity. 1998 Mar;8(3):305-17. PMID:9529148^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Fremont DH, Monnaie D, Nelson CA, Hendrickson WA, Unanue ER. Crystal structure of I-Ak in complex with a dominant epitope of lysozyme. Immunity. 1998 Mar;8(3):305-17. PMID:9529148

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1iak"

Categories: Large Structures | Mus musculus | Fremont DH | Hendrickson WA | Unanue ER

@@ Line 3: / Line 3: @@
 <StructureSection load='1iak' size='340' side='right'caption='[[1iak]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1iak]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IAK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IAK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1iak]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IAK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IAK FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 1.9&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=1iak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iak OCA], [https://pdbe.org/1iak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iak RCSB], [https://www.ebi.ac.uk/pdbsum/1iak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iak ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/LYSC_LOPLE LYSC_LOPLE]] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
+[https://www.uniprot.org/uniprot/HA2K_MOUSE HA2K_MOUSE]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 32: @@
 ==See Also==
 *[[MHC 3D structures|MHC 3D structures]]
+*[[MHC II 3D structures|MHC II 3D structures]]
 == References ==
 <references/>
@@ Line 36: / Line 38: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Fremont, D H]]
+[[Category: Fremont DH]]
-[[Category: Hendrickson, W A]]
+[[Category: Hendrickson WA]]
-[[Category: Unanue, E R]]
+[[Category: Unanue ER]]
-[[Category: Histocompatibility antigen]]
-[[Category: Histocompatibility antigen i-ak]]
-[[Category: Mhc]]
-[[Category: Peptide complex]]

1iak

From Proteopedia

Current revision

HISTOCOMPATIBILITY ANTIGEN I-AK

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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