. 2009 Jan;18(1):37–49. doi: 10.1002/pro.4

Table II.

Comparison of MHC Class I Structures in Liganded and Unliganded Forms

MHC molecule	HLA-A1	H-2K^b	HLA-A2	HLA-A2	HLA-B8	HLA-B*3508	H-2K^b	H-2K^b	H-2K^b	H-2K^b	H-2K^bm3	HLA-Cw4
Peptide	MAGE-A1	pOV8	p1049	Tax	FLR	LPEP	pKB1	VSV8	pBM1	dEV8	dEV8	C4CON1
Ligand	Fab-Hyb3	25-D1.16	TCR AHIII12.2	TCR A6	TCR LC13	TCR SB27	TCR KB5C20	TCR BM3.3	TCR BM3.3	TCR 2C	TCR 2C	KIR2DL1
PDB code, pMHC	3BO8^a	1VAC³³	1BOG³⁴	1HHK³⁵	1M05³⁶	1ZHL³⁷	1KJ3³⁸	2VAA³⁹	1NAN⁴⁰	1LEG⁴¹	1LEK⁴¹	1QQD⁴²
PDB code, pMHC:ligand	1W72¹⁴	3CVH⁴³	1LP9⁴⁴	1AO7¹⁶	1MI5⁴⁵	2AK4⁴⁶	1KJ2³⁸	1NAM⁴⁰	1FO0⁴⁷	2CKB⁴⁸	1MWA⁴¹	1IM9⁴
pMHC BSASA^b	990	1134	1193	1021	1135	1609	1482	1058	704	1093	1947	786
Comparisons of pMHC with pMHC:ligand complexes
HC residues contacting ligand	9	11	9	7	15	5	6	7	9	5	5	8
HC residues shifting >2.0 Å^c	4	4	1	3	5	4	2	4	1	1	2	2
Peptide residues contacting ligand	3	5	6	5	2	5	3	2	3	3	3	0
Peptide residues shifting >1.0 Å^d	0	3	0	4	1	2	0	1	0	5	5	0
Comparisons of rms deviation values (in Å) between pMHC and pMHC:ligand complexes
Peptide	0.37	0.34	0.24	1.01	0.28	0.36	0.14	0.14	0.29	0.63	0.45	0.23
HC^e	0.38	0.59	0.47	0.54	0.47	0.73	0.52	0.58	0.99	0.73	0.66	0.44
β₂m	0.32	0.88	0.50	0.42	0.38	0.37	0.43	1.36	1.66	0.89	0.75	0.40

This study.

Solvent accessible surface area of pMHC buried due to binding of its ligand.

Ligand-contacting HC residues with side chain apex shift ≥2 Å.

Peptide residues with side chain apex shift ≥1 Å.

Only the α1- and α2-domains of the HC are compared.

In those cases where more than one molecule within the asymmetric unit is present, only the first molecule has been analyzed.