2bck: Difference between revisions

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New page: left|200px<br /> <applet load="2bck" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bck, resolution 2.800Å" /> '''Crystal Structure ...
 
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[[Image:2bck.gif|left|200px]]<br /><applet load="2bck" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="2bck" size="450" color="white" frame="true" align="right" spinBox="true"  
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'''Crystal Structure of HLA-A*2402 Complexed with a telomerase peptide'''<br />
'''Crystal Structure of HLA-A*2402 Complexed with a telomerase peptide'''<br />


==Overview==
==Overview==
HLA-A*2402 is the most commonly expressed HLA allele in oriental, populations. It is also widely expressed in the Caucasian population, making it one of, if not the most abundant HLA I types. In order to study, its structure in terms of overall fold and peptide presentation, a soluble, form of this HLA I (alpha1, alpha2, alpha3 and beta(2)m domains) has been, expressed, refolded and crystallized in complex with a cancer-related, telomerase peptide (VYGFVRACL), and its structure has been solved to 2.8 A, resolution. The overall structure of HLA-A*2402 is virtually identical to, other reported peptide-HLA I structures. However, there are distinct, features observable from this structure at the HLA I peptide binding, pockets. The size and depth of pocket B makes it highly suitable for, binding to large aromatic side chains, which explains the high prevalence, of tyrosine at peptide position 2. Also, for HLA binding at peptide, position 5, there is an additional anchor point, which allows the proximal, amino acids to protrude out, providing a prominent feature for TCR, interaction. Finally, pocket F allows the anchor residue at position 9 to, be bound unusually deeply within the HLA structure.
HLA-A*2402 is the most commonly expressed HLA allele in oriental populations. It is also widely expressed in the Caucasian population, making it one of, if not the most abundant HLA I types. In order to study its structure in terms of overall fold and peptide presentation, a soluble form of this HLA I (alpha1, alpha2, alpha3 and beta(2)m domains) has been expressed, refolded and crystallized in complex with a cancer-related telomerase peptide (VYGFVRACL), and its structure has been solved to 2.8 A resolution. The overall structure of HLA-A*2402 is virtually identical to other reported peptide-HLA I structures. However, there are distinct features observable from this structure at the HLA I peptide binding pockets. The size and depth of pocket B makes it highly suitable for binding to large aromatic side chains, which explains the high prevalence of tyrosine at peptide position 2. Also, for HLA binding at peptide position 5, there is an additional anchor point, which allows the proximal amino acids to protrude out, providing a prominent feature for TCR interaction. Finally, pocket F allows the anchor residue at position 9 to be bound unusually deeply within the HLA structure.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
2BCK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/RNA-directed_DNA_polymerase RNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.49 2.7.7.49] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BCK OCA].  
2BCK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/RNA-directed_DNA_polymerase RNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.49 2.7.7.49] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BCK OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: RNA-directed DNA polymerase]]
[[Category: RNA-directed DNA polymerase]]
[[Category: Cole, D.K.]]
[[Category: Cole, D K.]]
[[Category: Gao, G.F.]]
[[Category: Gao, G F.]]
[[Category: Jakobsen, B.K.]]
[[Category: Jakobsen, B K.]]
[[Category: Rizkallah, P.J.]]
[[Category: Rizkallah, P J.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: mhc fold]]
[[Category: mhc fold]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:00:57 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:36:20 2008''

Revision as of 17:36, 21 February 2008

File:2bck.gif


2bck, resolution 2.800Å

Drag the structure with the mouse to rotate

Crystal Structure of HLA-A*2402 Complexed with a telomerase peptide

OverviewOverview

HLA-A*2402 is the most commonly expressed HLA allele in oriental populations. It is also widely expressed in the Caucasian population, making it one of, if not the most abundant HLA I types. In order to study its structure in terms of overall fold and peptide presentation, a soluble form of this HLA I (alpha1, alpha2, alpha3 and beta(2)m domains) has been expressed, refolded and crystallized in complex with a cancer-related telomerase peptide (VYGFVRACL), and its structure has been solved to 2.8 A resolution. The overall structure of HLA-A*2402 is virtually identical to other reported peptide-HLA I structures. However, there are distinct features observable from this structure at the HLA I peptide binding pockets. The size and depth of pocket B makes it highly suitable for binding to large aromatic side chains, which explains the high prevalence of tyrosine at peptide position 2. Also, for HLA binding at peptide position 5, there is an additional anchor point, which allows the proximal amino acids to protrude out, providing a prominent feature for TCR interaction. Finally, pocket F allows the anchor residue at position 9 to be bound unusually deeply within the HLA structure.

DiseaseDisease

Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[142800], Ankylosing spondylitis, susceptibility to, 1 OMIM:[142800], Aplastic anemia, susceptibility to OMIM:[187270], Dyskeratosis congenita OMIM:[187270], Hypoproteinemia, hypercatabolic OMIM:[109700], Pulmonary fibrosis,idiopathic, susceptibility to OMIM:[187270], Stevens-Johnson syndrome, susceptibility to OMIM:[142800]

About this StructureAbout this Structure

2BCK is a Protein complex structure of sequences from Homo sapiens with and as ligands. Active as RNA-directed DNA polymerase, with EC number 2.7.7.49 Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of HLA-A*2402 complexed with a telomerase peptide., Cole DK, Rizkallah PJ, Gao F, Watson NI, Boulter JM, Bell JI, Sami M, Gao GF, Jakobsen BK, Eur J Immunol. 2006 Jan;36(1):170-9. PMID:16323248

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